1WU9

Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)

Summary for 1WU9

• Entry DOI: 10.2210/pdb1wu9/pdb
• Descriptor: Microtubule-associated protein RP/EB family member 1 (2 entities in total)
• Functional Keywords: eb1-like structural motif, apc/dynactin binding domain, coiled coil, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: Q15691
• Total number of polymer chains: 2
• Total formula weight: 18424.06

Authors

Honnappa, S.,John, C.M.,Kostrewa, D.,Winkler, F.K.,Steinmetz, M.O. (deposition date: 2004-12-02, release date: 2005-02-01, Last modification date: 2024-03-13)

Primary citation

Honnappa, S.,John, C.M.,Kostrewa, D.,Winkler, F.K.,Steinmetz, M.O.
Structural insights into the EB1-APC interaction
Embo J., 24:261-269, 2005

PubMed Abstract: 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.

PubMed: 15616574
DOI: 10.1038/sj.emboj.7600529

Experimental method

X-RAY DIFFRACTION (1.54 Å)