2J6F

N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B PEPTIDE

Summary for 2J6F

• Entry DOI: 10.2210/pdb2j6f/pdb
• Related: 2J6K 2J6O 2J7I
• Descriptor: CD2-ASSOCIATED PROTEIN, E3 UBIQUITIN-PROTEIN LIGASE CBL-B (3 entities in total)
• Functional Keywords: metal-binding, immune response, sh3, ligase, sh2 domain, sh3 domain, zinc-finger, sh3- binding, ubl conjugation pathway, cytoskeletal rearrangements, phosphorylation, adaptor protein, egfr downregulation, cd2 associated protein, protein binding
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 2
• Total formula weight: 8744.91

Authors

Moncalian, G.,Cardenes, N.,Deribe, Y.L.,Spinola-Amilibia, M.,Dikic, I.,Bravo, J. (deposition date: 2006-09-28, release date: 2006-10-11, Last modification date: 2024-05-08)

Primary citation

Moncalian, G.,Cardenes, N.,Deribe, Y.L.,Spinola-Amilibia, M.,Dikic, I.,Bravo, J.
Atypical Polyproline Recognition by the Cms N- Terminal SH3 Domain.
J.Biol.Chem., 281:38845-, 2006

PubMed Abstract: 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.

PubMed: 17020880
DOI: 10.1074/JBC.M606411200

Experimental method

X-RAY DIFFRACTION (1.7 Å)