1wu9
From Proteopedia
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Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)
Overview
EB1 proteins bind to microtubule ends where they act in concert with other, components, including the adenomatous polyposis coli (APC) tumor, suppressor, to regulate the microtubule filament system. We find that EB1, is a stable dimer with a parallel coiled coil and show that dimerization, is essential for the formation of its C-terminal domain (EB1-C). The, crystal structure of EB1-C reveals a highly conserved surface patch with a, deep hydrophobic cavity at its center. EB1-C binds two copies of an, APC-derived C-terminal peptide (C-APCp1) with equal 5 microM affinity. The, conserved APC Ile2805-Pro2806 sequence motif serves as an anchor for the, interaction of C-APCp1 with the hydrophobic cavity of EB1-C., Phosphorylation of the conserved Cdc2 site Ser2789-Lys2792 in C-APCp1, reduces binding four-fold, indicating that the interaction APC-EB1 is, post-translationally regulated in cells. Our findings provide a basis for, understanding the dynamic crosstalk of EB1 proteins with their molecular, targets in eukaryotic organisms.
About this Structure
1WU9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural insights into the EB1-APC interaction., Honnappa S, John CM, Kostrewa D, Winkler FK, Steinmetz MO, EMBO J. 2005 Jan 26;24(2):261-9. Epub 2004 Dec 23. PMID:15616574
Page seeded by OCA on Mon Nov 12 19:54:57 2007
