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==Overview==
==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.
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==
==About this Structure==
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[[Category: Bravo, J.]]
[[Category: Bravo, J.]]
[[Category: Cardenes, N.]]
[[Category: Cardenes, N.]]
[[Category: Deribe, Y.L.]]
[[Category: Deribe, Y L.]]
[[Category: Dikic, I.]]
[[Category: Dikic, I.]]
[[Category: Moncalian, G.]]
[[Category: Moncalian, G.]]
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[[Category: transmembrane]]
[[Category: transmembrane]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:08 2008''

Revision as of 16:00, 21 February 2008

File:2j7i.jpg


2j7i, resolution 2.90Å

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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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