1yig
From Proteopedia
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Crystal Structure of the Human EB1 C-terminal Dimerization Domain
Overview
EB1 is a member of a conserved protein family that localizes to growing, microtubule plus ends. EB1 proteins also recruit cell polarity and, signaling molecules to microtubule tips. However, the mechanism by which, EB1 recognizes cargo is unknown. Here, we have defined a repeat sequence, in adenomatous polyposis coli (APC) that binds to EB1's COOH-terminal, domain and identified a similar sequence in members of the microtubule, actin cross-linking factor (MACF) family of spectraplakins. We show that, MACFs directly bind EB1 and exhibit EB1-dependent plus end tracking in, vivo. To understand how EB1 recognizes APC and MACFs, we solved the, crystal structure of the EB1 COOH-terminal domain. The structure reveals a, novel homodimeric fold comprised of a coiled coil and four-helix bundle, motif. Mutational analysis reveals that the cargo binding site for MACFs, maps to a cluster of conserved residues at the junction between the coiled, coil and four-helix bundle. These results provide a structural, understanding of how EB1 binds two regulators of microtubule-based cell, polarity.
About this Structure
1YIG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end., Slep KC, Rogers SL, Elliott SL, Ohkura H, Kolodziej PA, Vale RD, J Cell Biol. 2005 Feb 14;168(4):587-98. Epub 2005 Feb 7. PMID:15699215
Page seeded by OCA on Mon Nov 12 20:20:24 2007
