| http://purl.uniprot.org/citations/17020880 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17020880 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17020880 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m606411200"xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m606411200"xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Bravo J."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Bravo J."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Dikic I."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Dikic I."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Moncalian G."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Moncalian G."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Cardenes N."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Cardenes N."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Deribe Y.L."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Deribe Y.L."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Spinola-Amilibia M."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/author | "Spinola-Amilibia M."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/pages | "38845-38853"xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/pages | "38845-38853"xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/title | "Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain."xsd:string |
| http://purl.uniprot.org/citations/17020880 | http://purl.uniprot.org/core/title | "Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain."xsd:string |