2j6k

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[[Image:2j6k.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6k OCA], [http://www.ebi.ac.uk/pdbsum/2j6k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j6k RCSB]</span>
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'''N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG)'''
'''N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG)'''
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[[Category: Moncalian, G.]]
[[Category: Moncalian, G.]]
[[Category: Spinola-Amilibia, M.]]
[[Category: Spinola-Amilibia, M.]]
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[[Category: adaptor protein]]
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[[Category: Adaptor protein]]
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[[Category: cd2 associated protein]]
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[[Category: Cd2 associated protein]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: cytoskeletal rearrangement]]
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[[Category: Cytoskeletal rearrangement]]
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[[Category: egfr downregulation]]
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[[Category: Egfr downregulation]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: protein binding]]
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[[Category: Protein binding]]
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[[Category: sh3]]
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[[Category: Sh3]]
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[[Category: sh3 domain]]
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[[Category: Sh3 domain]]
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[[Category: sh3-binding]]
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[[Category: Sh3-binding]]
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[[Category: signaling protein]]
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[[Category: Signaling protein]]
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[[Category: surface active protein]]
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[[Category: Surface active protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:43 2008''
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Revision as of 05:25, 4 May 2008

Template:STRUCTURE 2j6k

N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG)


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

2J6K is a Single protein structure of sequence 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 Page seeded by OCA on Sun May 4 08:25:10 2008

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