2j7i | pdb_00002j7i

File:2j7i.gif

spinqualitylabelsall models 2j7i, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3 DOMAIN. CMS:CD2 HETERODIMER

Overview

The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic, adaptor proteins has the ability to engage multiple effectors and couple, cargo trafficking with the cytoskeleton. CIN85 and CMS (Cas ligand with, multiple Src homology 3 (SH3) domains) facilitate the formation of large, multiprotein complexes required for an efficient internalization of cell, surface receptors. It has recently been shown that c-Cbl/Cbl-b could, mediate the formation of a ternary complex between one c-Cbl/Cbl-b, molecule and two SH3 domains of CIN85, important for the ability of Cbl to, promote epidermal growth factor receptor down-regulation. To further, investigate whether multimerization is conserved within the family of, adaptor proteins, we have solved the crystal structures of the CMS, N-terminal SH3 domain-forming complexes with Cbl-b- and CD2-derived, peptides. Together with biochemical evidence, the structures support the, notion that, despite clear differences in the interaction surface, both, Cbl-b and CD2 can mediate multimerization of N-terminal CMS SH3 domains., Detailed analyses on the interacting surfaces also provide the basis for a, differential Cbl-b molecular recognition of CMS and CIN85.

About this Structure

2J7I is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain., Moncalian G, Cardenes N, Deribe YL, Spinola-Amilibia M, Dikic I, Bravo J, J Biol Chem. 2006 Dec 15;281(50):38845-53. Epub 2006 Oct 3. PMID:17020880

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