2j6k: Difference between revisions

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[[Image:2j6k.jpg|left|200px]]
{{Seed}}
[[Image:2j6k.png|left|200px]]


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{{STRUCTURE_2j6k|  PDB=2j6k  |  SCENE=  }}  
{{STRUCTURE_2j6k|  PDB=2j6k  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_17020880}}


==About this Structure==
==About this Structure==
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[[Category: Signaling protein]]
[[Category: Signaling protein]]
[[Category: Surface active protein]]
[[Category: Surface active protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:25:10 2008''
 
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Revision as of 01:52, 28 July 2008

File:2j6k.png

Template:STRUCTURE 2j6k

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

Template:ABSTRACT PUBMED 17020880

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

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