Crystal Structure of the Amino-terminal Microtubule-binding Domain of End-binding Protein 1 (EB1)

The end-binding protein 1 (EB1) family is a highly conserved group of proteins that localizes to the plus-ends of microtubules. EB1 has been shown to play an important role in regulating microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly understood. We have determined the 1.45-Å resolution crystal structure of the amino-terminal domain of EB1, which is essential for microtubule binding, and show that it forms a calponin homology (CH) domain fold that is found in many proteins involved in the actin cytoskeleton. The functional CH domain for actin binding is a tandem pair, whereas EB1 is the first example of a single CH domain that can associate with the microtubule filament. Although our biochemical study shows that microtubule binding of EB1 is electrostatic in part, our mutational analysis suggests that the hydrophobic network, which is partially exposed in our crystal structure, is also important for the association. We propose that, like other actin-binding CH domains, EB1 employs the hydrophobic interaction to bind to microtubules. The end-binding protein 1 (EB1) family is a highly conserved group of proteins that localizes to the plus-ends of microtubules. EB1 has been shown to play an important role in regulating microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly understood. We have determined the 1.45-Å resolution crystal structure of the amino-terminal domain of EB1, which is essential for microtubule binding, and show that it forms a calponin homology (CH) domain fold that is found in many proteins involved in the actin cytoskeleton. The functional CH domain for actin binding is a tandem pair, whereas EB1 is the first example of a single CH domain that can associate with the microtubule filament. Although our biochemical study shows that microtubule binding of EB1 is electrostatic in part, our mutational analysis suggests that the hydrophobic network, which is partially exposed in our crystal structure, is also important for the association. We propose that, like other actin-binding CH domains, EB1 employs the hydrophobic interaction to bind to microtubules. Microtubules (MTs) 1The abbreviations used are: MT, microtubule; MAP, microtubule-associated protein; APC, adenomatous polyposis coli; CH domain, calponin homology domain; CAP-Gly, glycine-rich cytoskeleton-associated protein; En, EB1 MT-binding domain; MES, 4-morpho-lineethanesulfonic acid; PIPES, piperazine-N,N′-bis(2-ethanesulfonic acid); r.m.s.d., root-mean-square deviation.1The abbreviations used are: MT, microtubule; MAP, microtubule-associated protein; APC, adenomatous polyposis coli; CH domain, calponin homology domain; CAP-Gly, glycine-rich cytoskeleton-associated protein; En, EB1 MT-binding domain; MES, 4-morpho-lineethanesulfonic acid; PIPES, piperazine-N,N′-bis(2-ethanesulfonic acid); r.m.s.d., root-mean-square deviation. are an essential component of the cytoskeleton, underlying the fundamental processes of cell morphogenesis, cell motility, and cell division. The organization and dynamics of MT polymers are highly regulated, and numerous proteins including MT-associated proteins (MAPs) and molecular motors have been proposed as possible regulatory factors (1Desai A. Mitchison T.J. Annu. Rev. Cell Dev. Biol. 1997; 13: 83-117Crossref PubMed Scopus (1924) Google Scholar).MTs have an intrinsic structural polarity, consisting of a highly dynamic plus-end toward the cell periphery and a centrosome-associated minus-end. Their dynamics involve alternating phases of growth and shortening, known as dynamic instability (2Mitchison T. Kirschner M. Nature. 1984; 312: 237-242Crossref PubMed Scopus (2291) Google Scholar). Dynamic instability is modulated by various MAPs and motor proteins, some of which act to promote MT assembly and stability, whereas others induce their depolymerization (3Desai A. Verma S. Mitchison T.J. Walczak C.E. Cell. 1999; 96: 69-78Abstract Full Text Full Text PDF PubMed Scopus (576) Google Scholar). Two groups of proteins that specifically bind to the MT plus-ends, termed “plus-end-tracking proteins” or +TIPs (4Schuyler S. Pellman D. Cell. 2001; 105: 421-424Abstract Full Text Full Text PDF PubMed Scopus (319) Google Scholar) have been identified: the CAP-Gly proteins (e.g. CLIP-170, p150glued of dynactin) and the EB1 family proteins (5Perez F. Diamantopoulos G.S. Stalder R. Kreis T.E. Cell. 1999; 96: 517-527Abstract Full Text Full Text PDF PubMed Scopus (324) Google Scholar, 6Vaughan K.T. Tynan S.H. Faulkner N.E. Echeverri C.J. Vallee R.B. J. Cell Sci. 1999; 112: 1437-1447Crossref PubMed Google Scholar, 7Berrueta L. Kraeft S.K. Tirnauer J.S. Schuyler S.C. Chen L.B. Hill D.E. Pellman D. Bierer B.E. Proc. Natl. Acad. Sci. U. S. A. 1998; 95: 10596-10601Crossref PubMed Scopus (154) Google Scholar). Although they can bind to MTs independently, evidence for interactions among them have led to the hypothesis of a “plus-end complex” (8Schroer T.A. Curr. Opin. Cell Biol. 2001; 13: 92-96Crossref PubMed Scopus (66) Google Scholar, 9Ligon L.A. Shelly S.S. Tokito M. Holzbaur E.L. Mol. Biol. Cell. 2003; 14: 1405-1417Crossref PubMed Scopus (152) Google Scholar). The main function of a plus-end complex may be the regulation of MT dynamics, but the mechanisms are poorly understood.EB1 was initially identified in a yeast two-hybrid screen by its binding to the carboxyl terminus of the adenomatous polyposis coli (APC) tumor suppressor protein (10Su L.K. Burrell M. Hill D.E. Gyuris J. Brent R. Wiltshire R. Trent J. Vogelstein B. Kinzler K.W. Cancer Res. 1995; 55: 2972-2977PubMed Google Scholar), which may be essential for the tumor-suppressing function of APC (11Kinzler K.W. Vogelstein B. Cell. 1996; 87: 159-170Abstract Full Text Full Text PDF PubMed Scopus (4252) Google Scholar). Proteins homologous to EB1 have been identified in many yeast to and have been shown to with MT plus-ends K.T. Tynan S.H. Faulkner N.E. Echeverri C.J. Vallee R.B. J. Cell Sci. 1999; 112: 1437-1447Crossref PubMed Google Scholar, U. J. Cell Biol. 1997; PubMed Scopus Google Scholar, D. Mol. Biol. Cell. 1997; PubMed Scopus Google Scholar, 1998; PubMed Scopus Google Scholar, A. A. M. J. 1999; PubMed Scopus Google Scholar). EB1 binding to MTs is of APC, but APC to MT plus-ends EB1 PubMed Scopus Google Scholar, S. Curr. Biol. Full Text Full Text PDF PubMed Scopus Google Scholar). the APC carboxyl terminus with EB1 to MTs M. Curr. Biol. 2001; Full Text Full Text PDF PubMed Scopus Google have that EB1 of an amino-terminal MT-binding domain and a domain Cell Sci. Google Scholar, K.T. Mol. Biol. Cell. 13: PubMed Scopus Google Scholar). the structural of EB1 function in MT binding, have determined the crystal structure of The structural with the calponin homology domain led to the MT binding of with that the interaction is hydrophobic and electrostatic in and EB1 amino-terminal MT-binding domain was by a and and The protein with was in coli Cell was to a The protein was with to the and by with a and 1 The protein to in the as in and used for proteins as C.J. PubMed Scopus Google Scholar) and as for the the The of the by in coli and as for the by a of protein with an of The of the group a with and MES, crystal was a and crystal forms in the to a in their and in a the and with and 1997; Scholar). was used to in the crystal and to the phases The phases to and by Biol. PubMed Scopus Google Scholar). molecular was a of in the was with the Biol. PubMed Scopus Google Scholar). The was D.E. J. Biol. 1999; PubMed Scopus Google Scholar). The was by Biol. PubMed Scopus Google Scholar). The structure of crystal was by molecular with the J. M. T. Biol. 1998; PubMed Scopus Google Scholar) the crystal structure as a was in PIPES, 1 with a of for was to with and for of was with of or its and for to was by a for in an in and by with of to the EB1 protein a domain, amino-terminal that the MT-binding domain as Cell Sci. Google Scholar, K.T. Mol. Biol. Cell. 13: PubMed Scopus Google Scholar). of of which to The to and the structure was determined by a was for The structure of a crystal was determined to by molecular the first structure as a We for in the and carboxyl and cell in to for the of in to for the of in to for the of is the and is the for of of in and for in the and The was a of the that was of of protein of of other in to for the of is the and is the for 1997; and for in the and The was a of the that was of in a The structure which is with of The of the domain is by and The first forms an of with the and and a to a hydrophobic and are partially exposed to the a conserved hydrophobic that a protein interaction MT-binding of a in the and with conserved in many MAPs a and are proposed to bind to the of R. and Scholar). The of with the of in a of The structure was a with the shown in electrostatic of to of The hydrophobic is shown in and the in highly conserved conserved The hydrophobic is by a with A. B. PubMed Scopus Google of and EB1 and are with other actin-binding CH is shown with structural are the The actin-binding in study and are in The to and are in to and in and to in the L. Res. 1997; PubMed Scopus Google Scholar), found that the structure has a calponin homology (CH) domain fold as in many actin-binding proteins The proteins are root-mean-square S. M. 1996; Full Text Full Text PDF Scopus Google Scholar), for S.C. S.C. Biol. 1997; PubMed Scopus Google Scholar), and calponin for J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The structure is conserved among the CH domains, has its and carboxyl of structure is with of and are shown in are the as in are the and tandem of CH domains, consisting of has been to actin binding a of and J. M. 1995; PubMed Scopus Google Scholar). Although a EB1 to with other CH domains, some of the in the are conserved the CH domain family that they are essential for the in EB1 is the CH domain family J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The of forms interactions with the of and the of and are conserved as the hydrophobic in the EB1 our crystal structure, found that and are exposed to to the of and is found in for the of protein that be of the to MT by which in the and is conserved as or in many to known The and are in the and among the of EB1 have been and the regulation of EB1 in have a that is to be important for binding to the of is the of an for MAPs R. and Scholar). the other the actin-binding in many CH are hydrophobic in S.C. S.C. Biol. 1997; PubMed Scopus Google Scholar, M. PubMed Scopus Google Scholar), which to of the first CH domain of the tandem and and of the our crystal structure, MT-binding the with the and and the conserved hydrophobic by and the interaction EB1 and MTs is MT-binding with various with MTs the bind suggests that the binding in part, of with of with MTs in various the of with mutational analysis of the interaction and to MTs is shown in the whereas the shows the of the of the of is in and the hydrophobic are in the MT-binding En, and single and to a electrostatic and are in the whereas is to the hydrophobic as by and with whereas binding crystal structure shows that the of highly conserved is and hydrophobic in EB1 its is in the of the of and forms a interaction with the of a of structure, in the of in coli propose that the hydrophobic for MT binding as as for the of the CH domain yeast study of the EB1 that the of the interaction is the carboxyl terminus of D. Mol. Biol. Cell. 1997; PubMed Scopus Google Scholar). show that binding is electrostatic but also that the hydrophobic may be the main binding for The of the has a conserved the carboxyl which may as a for the hydrophobic crystal structure of MT the CAP-Gly domain, structural with S. J. S.H. Chen M. J. D. J. L.A. B. M. J. Biol. Full Text Full Text PDF PubMed Scopus Google Scholar). the CAP-Gly domain structure, an is in a by which is proposed to MT be that is a conserved hydrophobic the or structural analysis is to a mechanism of plus-end CH domain is as a protein interaction in a of the functional CH domain for actin binding is to be a tandem pair, whereas the actin-binding of the single CH domain is J. D. Full Text Full Text PDF PubMed Scopus Google Scholar, M. PubMed Scopus Google Scholar). is the first example of a single CH domain that can bind to the filament. We propose that, to actin-binding CH domains, employs hydrophobic interactions to bind to Microtubules (MTs) 1The abbreviations used are: MT, microtubule; MAP, microtubule-associated protein; APC, adenomatous polyposis coli; CH domain, calponin homology domain; CAP-Gly, glycine-rich cytoskeleton-associated protein; En, EB1 MT-binding domain; MES, 4-morpho-lineethanesulfonic acid; PIPES, piperazine-N,N′-bis(2-ethanesulfonic acid); r.m.s.d., root-mean-square deviation.1The abbreviations used are: MT, microtubule; MAP, microtubule-associated protein; APC, adenomatous polyposis coli; CH domain, calponin homology domain; CAP-Gly, glycine-rich cytoskeleton-associated protein; En, EB1 MT-binding domain; MES, 4-morpho-lineethanesulfonic acid; PIPES, piperazine-N,N′-bis(2-ethanesulfonic acid); r.m.s.d., root-mean-square deviation. are an essential component of the cytoskeleton, underlying the fundamental processes of cell morphogenesis, cell motility, and cell division. The organization and dynamics of MT polymers are highly regulated, and numerous proteins including MT-associated proteins (MAPs) and molecular motors have been proposed as possible regulatory factors (1Desai A. Mitchison T.J. Annu. Rev. Cell Dev. Biol. 1997; 13: 83-117Crossref PubMed Scopus (1924) Google Scholar). MTs have an intrinsic structural polarity, consisting of a highly dynamic plus-end toward the cell periphery and a centrosome-associated minus-end. Their dynamics involve alternating phases of growth and shortening, known as dynamic instability (2Mitchison T. Kirschner M. Nature. 1984; 312: 237-242Crossref PubMed Scopus (2291) Google Scholar). Dynamic instability is modulated by various MAPs and motor proteins, some of which act to promote MT assembly and stability, whereas others induce their depolymerization (3Desai A. Verma S. Mitchison T.J. Walczak C.E. Cell. 1999; 96: 69-78Abstract Full Text Full Text PDF PubMed Scopus (576) Google Scholar). Two groups of proteins that specifically bind to the MT plus-ends, termed “plus-end-tracking proteins” or +TIPs (4Schuyler S. Pellman D. Cell. 2001; 105: 421-424Abstract Full Text Full Text PDF PubMed Scopus (319) Google Scholar) have been identified: the CAP-Gly proteins (e.g. CLIP-170, p150glued of dynactin) and the EB1 family proteins (5Perez F. Diamantopoulos G.S. Stalder R. Kreis T.E. Cell. 1999; 96: 517-527Abstract Full Text Full Text PDF PubMed Scopus (324) Google Scholar, 6Vaughan K.T. Tynan S.H. Faulkner N.E. Echeverri C.J. Vallee R.B. J. Cell Sci. 1999; 112: 1437-1447Crossref PubMed Google Scholar, 7Berrueta L. Kraeft S.K. Tirnauer J.S. Schuyler S.C. Chen L.B. Hill D.E. Pellman D. Bierer B.E. Proc. Natl. Acad. Sci. U. S. A. 1998; 95: 10596-10601Crossref PubMed Scopus (154) Google Scholar). Although they can bind to MTs independently, evidence for interactions among them have led to the hypothesis of a “plus-end complex” (8Schroer T.A. Curr. Opin. Cell Biol. 2001; 13: 92-96Crossref PubMed Scopus (66) Google Scholar, 9Ligon L.A. Shelly S.S. Tokito M. Holzbaur E.L. Mol. Biol. Cell. 2003; 14: 1405-1417Crossref PubMed Scopus (152) Google Scholar). The main function of a plus-end complex may be the regulation of MT dynamics, but the mechanisms are poorly understood. EB1 was initially identified in a yeast two-hybrid screen by its binding to the carboxyl terminus of the adenomatous polyposis coli (APC) tumor suppressor protein (10Su L.K. Burrell M. Hill D.E. Gyuris J. Brent R. Wiltshire R. Trent J. Vogelstein B. Kinzler K.W. Cancer Res. 1995; 55: 2972-2977PubMed Google Scholar), which may be essential for the tumor-suppressing function of APC (11Kinzler K.W. Vogelstein B. Cell. 1996; 87: 159-170Abstract Full Text Full Text PDF PubMed Scopus (4252) Google Scholar). Proteins homologous to EB1 have been identified in many yeast to and have been shown to with MT plus-ends K.T. Tynan S.H. Faulkner N.E. Echeverri C.J. Vallee R.B. J. Cell Sci. 1999; 112: 1437-1447Crossref PubMed Google Scholar, U. J. Cell Biol. 1997; PubMed Scopus Google Scholar, D. Mol. Biol. Cell. 1997; PubMed Scopus Google Scholar, 1998; PubMed Scopus Google Scholar, A. A. M. J. 1999; PubMed Scopus Google Scholar). EB1 binding to MTs is of APC, but APC to MT plus-ends EB1 PubMed Scopus Google Scholar, S. Curr. Biol. Full Text Full Text PDF PubMed Scopus Google Scholar). the APC carboxyl terminus with EB1 to MTs M. Curr. Biol. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar). have that EB1 of an amino-terminal MT-binding domain and a domain Cell Sci. Google Scholar, K.T. Mol. Biol. Cell. 13: PubMed Scopus Google Scholar). the structural of EB1 function in MT binding, have determined the crystal structure of The structural with the calponin homology domain led to the MT binding of with that the interaction is hydrophobic and electrostatic in and EB1 amino-terminal MT-binding domain was by a and and The protein with was in coli Cell was to a The protein was with to the and by with a and 1 The protein to in the as in and used for proteins as C.J. PubMed Scopus Google Scholar) and as for the the The of the by in coli and as for the by a of protein with an of The of the group a with and MES, crystal was a and crystal forms in the to a in their and in a the and with and 1997; Scholar). was used to in the crystal and to the phases The phases to and by Biol. PubMed Scopus Google Scholar). molecular was a of in the was with the Biol. PubMed Scopus Google Scholar). The was D.E. J. Biol. 1999; PubMed Scopus Google Scholar). The was by Biol. PubMed Scopus Google Scholar). The structure of crystal was by molecular with the J. M. T. Biol. 1998; PubMed Scopus Google Scholar) the crystal structure as a was in PIPES, 1 with a of for was to with and for of was with of or its and for to was by a for in an in and by with and EB1 amino-terminal MT-binding domain was by a and and The protein with was in coli Cell was to a The protein was with to the and by with a and 1 The protein to in the as in and used for proteins as C.J. PubMed Scopus Google Scholar) and as for the the The of the by in coli and as for the by a of protein with an of The of the group a with and MES, crystal was a and crystal forms in the to a in their and in a the and with and 1997; Scholar). was used to in the crystal and to the phases The phases to and by Biol. PubMed Scopus Google Scholar). molecular was a of in the was with the Biol. PubMed Scopus Google Scholar). The was D.E. J. Biol. 1999; PubMed Scopus Google Scholar). The was by Biol. PubMed Scopus Google Scholar). The structure of crystal was by molecular with the J. M. T. Biol. 1998; PubMed Scopus Google Scholar) the crystal structure as a was in PIPES, 1 with a of for was to with and for of was with of or its and for to was by a for in an in and by with of to the EB1 protein a domain, amino-terminal that the MT-binding domain as Cell Sci. Google Scholar, K.T. Mol. Biol. Cell. 13: PubMed Scopus Google Scholar). of of which to The to and the structure was determined by a was for The structure of a crystal was determined to by molecular the first structure as a We for in the and carboxyl and cell in to for the of in to for the of in to for the of is the and is the for of of in and for in the and The was a of the that was of of protein of of other in to for the of is the and is the for 1997; and for in the and The was a of the that was of in a The structure which is with of The of the domain is by and The first forms an of with the and and a to a hydrophobic and are partially exposed to the a conserved hydrophobic that a protein interaction MT-binding of a in the and with conserved in many MAPs a and are proposed to bind to the of R. and Scholar). The of with the of in a of and EB1 and are with other actin-binding CH is shown with structural are the The actin-binding in study and are in The to and are in to and in and to in the L. Res. 1997; PubMed Scopus Google Scholar), found that the structure has a calponin homology (CH) domain fold as in many actin-binding proteins The proteins are root-mean-square S. M. 1996; Full Text Full Text PDF Scopus Google Scholar), for S.C. S.C. Biol. 1997; PubMed Scopus Google Scholar), and calponin for J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The structure is conserved among the CH domains, has its and carboxyl of structure is with of and are shown in are the as in are the and tandem of CH domains, consisting of has been to actin binding a of and J. M. 1995; PubMed Scopus Google Scholar). Although a EB1 to with other CH domains, some of the in the are conserved the CH domain family that they are essential for the in EB1 is the CH domain family J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The of forms interactions with the of and the of and are conserved as the hydrophobic in the EB1 our crystal structure, found that and are exposed to to the of and is found in for the of protein that be of the to MT by which in the and is conserved as or in many to known The and are in the and among the of EB1 have been and the regulation of EB1 in have a that is to be important for binding to the of is the of an for MAPs R. and Scholar). the other the actin-binding in many CH are hydrophobic in S.C. S.C. Biol. 1997; PubMed Scopus Google Scholar, M. PubMed Scopus Google Scholar), which to of the first CH domain of the tandem and and of the our crystal structure, MT-binding the with the and and the conserved hydrophobic by and the interaction EB1 and MTs is MT-binding with various with MTs the bind suggests that the binding in part, of with of with MTs in various the of with mutational analysis of the interaction and to MTs is shown in the whereas the shows the of the of the of is in and the hydrophobic are in the MT-binding En, and single and to a electrostatic and are in the whereas is to the hydrophobic as by and with whereas binding crystal structure shows that the of highly conserved is and hydrophobic in EB1 its is in the of the of and forms a interaction with the of a of structure, in the of in coli propose that the hydrophobic for MT binding as as for the of the CH domain yeast study of the EB1 that the of the interaction is the carboxyl terminus of D. Mol. Biol. Cell. 1997; PubMed Scopus Google Scholar). show that binding is electrostatic but also that the hydrophobic may be the main binding for The of the has a conserved the carboxyl which may as a for the hydrophobic crystal structure of MT the CAP-Gly domain, structural with S. J. S.H. Chen M. J. D. J. L.A. B. M. J. Biol. Full Text Full Text PDF PubMed Scopus Google Scholar). the CAP-Gly domain structure, an is in a by which is proposed to MT be that is a conserved hydrophobic the or structural analysis is to a mechanism of plus-end CH domain is as a protein interaction in a of the functional CH domain for actin binding is to be a tandem pair, whereas the actin-binding of the single CH domain is J. D. Full Text Full Text PDF PubMed Scopus Google Scholar, M. PubMed Scopus Google Scholar). is the first example of a single CH domain that can bind to the filament. We propose that, to actin-binding CH domains, employs hydrophobic interactions to bind to of to the EB1 protein a domain, amino-terminal that the MT-binding domain as Cell Sci. Google Scholar, K.T. Mol. Biol. Cell. 13: PubMed Scopus Google Scholar). of of which to The to and the structure was determined by a was for The structure of a crystal was determined to by molecular the first structure as a We for in the and carboxyl and The structure which is with of The of the domain is by and The first forms an of with the and and a to a hydrophobic and are partially exposed to the a conserved hydrophobic that a protein interaction MT-binding of a in the and with conserved in many MAPs a and are proposed to bind to the of R. and Scholar). The of with the of in a the L. Res. 1997; PubMed Scopus Google Scholar), found that the structure has a calponin homology (CH) domain fold as in many actin-binding proteins The proteins are root-mean-square S. M. 1996; Full Text Full Text PDF Scopus Google Scholar), for S.C. S.C. Biol. 1997; PubMed Scopus Google Scholar), and calponin for J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The structure is conserved among the CH domains, has its and carboxyl tandem of CH domains, consisting of has been to actin binding a of and J. M. 1995; PubMed Scopus Google Scholar). Although a EB1 to with other CH domains, some of the in the are conserved the CH domain family that they are essential for the in EB1 is the CH domain family J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The of forms interactions with the of and the of and are conserved as the hydrophobic in the EB1 our crystal structure, found that and are exposed to to the of and is found in for the of protein that be of the to MT by which in the and is conserved as or in many to known The and are in the and among the of EB1 have been and the regulation of EB1 in have a that is to be important for binding to the of is the of an for MAPs R. and Scholar). the other the actin-binding in many CH are hydrophobic in S.C. S.C. Biol. 1997; PubMed Scopus Google Scholar, M. PubMed Scopus Google Scholar), which to of the first CH domain of the tandem and and of the our crystal structure, MT-binding the with the and and the conserved hydrophobic by and the interaction EB1 and MTs is MT-binding with various with MTs the bind suggests that the binding in part, the MT-binding En, and single and to a electrostatic and are in the whereas is to the hydrophobic as by and with whereas binding crystal structure shows that the of highly conserved is and hydrophobic in EB1 its is in the of the of and forms a interaction with the of a of structure, in the of in coli propose that the hydrophobic for MT binding as as for the of the CH domain yeast study of the EB1 that the of the interaction is the carboxyl terminus of D. Mol. Biol. Cell. 1997; PubMed Scopus Google Scholar). show that binding is electrostatic but also that the hydrophobic may be the main binding for The of the has a conserved the carboxyl which may as a for the hydrophobic crystal structure of MT the CAP-Gly domain, structural with S. J. S.H. Chen M. J. D. J. L.A. B. M. J. Biol. Full Text Full Text PDF PubMed Scopus Google Scholar). the CAP-Gly domain structure, an is in a by which is proposed to MT be that is a conserved hydrophobic the or structural analysis is to a mechanism of plus-end The CH domain is as a protein interaction in a of the functional CH domain for actin binding is to be a tandem pair, whereas the actin-binding of the single CH domain is J. D. Full Text Full Text PDF PubMed Scopus Google Scholar, M. PubMed Scopus Google Scholar). is the first example of a single CH domain that can bind to the filament. We propose that, to actin-binding CH domains, employs hydrophobic interactions to bind to We M. and for of the and the the for

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