2j7i
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Bravo, J.]] | [[Category: Bravo, J.]] | ||
[[Category: Cardenes, N.]] | [[Category: Cardenes, N.]] | ||
| - | [[Category: Deribe, Y | + | [[Category: Deribe, Y L.]] |
[[Category: Dikic, I.]] | [[Category: Dikic, I.]] | ||
[[Category: Moncalian, G.]] | [[Category: Moncalian, G.]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:08 2008'' |
Revision as of 16:00, 21 February 2008
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ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3 DOMAIN. CMS:CD2 HETERODIMER
Overview
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.
About this Structure
2J7I is a Protein complex structure of sequences 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
Page seeded by OCA on Thu Feb 21 18:00:08 2008
Categories: Homo sapiens | Protein complex | Bravo, J. | Cardenes, N. | Deribe, Y L. | Dikic, I. | Moncalian, G. | Spinola-Amilibia, M. | Adaptor protein | Cd2ad | Cell adhesion | Cms | Coiled coil | Egfr downregulation | Glycoprotein | Immunoglobulin domain | Membrane | Phosphorylation | Polymorphism | Protein binding | Sh3 domain | Sh3 domain recognition | Sh3-binding | Transmembrane
