2j7i: Difference between revisions

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[[Image:2j7i.jpg|left|200px]]
{{Seed}}
[[Image:2j7i.png|left|200px]]


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{{STRUCTURE_2j7i|  PDB=2j7i  |  SCENE=  }}  
{{STRUCTURE_2j7i|  PDB=2j7i  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_17020880}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17020880 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17020880}}


==About this Structure==
==About this Structure==
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[[Category: Sh3-binding]]
[[Category: Sh3-binding]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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