2J7I

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

Summary for 2J7I

• Entry DOI: 10.2210/pdb2j7i/pdb
• Related: 1CDB 1GYA 1HNF 1L2Z 2BZ8 2J6F 2J6K 2J6O
• Descriptor: CD2-ASSOCIATED PROTEIN, T-CELL SURFACE ANTIGEN CD2 (3 entities in total)
• Functional Keywords: coiled coil, polymorphism, glycoprotein, cell adhesion, egfr downregulation, immunoglobulin domain, transmembrane, phosphorylation, adaptor protein, cms, cd2ad, membrane, sh3 domain, sh3-binding, sh3 domain recognition, protein binding
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm, cytoskeleton : Q9Y5K6; Membrane; Single-pass type I membrane protein: P06729
• Total number of polymer chains: 4
• Total formula weight: 17063.33

Authors

Moncalian, G.,Cardenes, N.,Deribe, Y.L.,Spinola-Amilibia, M.,Dikic, I.,Bravo, J. (deposition date: 2006-10-09, release date: 2006-11-06, Last modification date: 2024-05-01)

Primary citation

Moncalian, G.,Cardenes, N.,Deribe, Y.L.,Spinola-Amilibia, M.,Dikic, I.,Bravo, J.
Atypical Polyproline Recognition by the Cms N-Terminal Src Homology 3 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 (2.9 Å)