2j6k
From Proteopedia
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==Overview== | ==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, ... | + | 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== | ||
| - | 2J6K is a | + | 2J6K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J6K OCA]. |
==Reference== | ==Reference== | ||
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[[Category: surface active protein]] | [[Category: surface active protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:51:48 2007'' |
Revision as of 10:46, 5 November 2007
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N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG)
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
2J6K is a Single protein structure of sequence from Homo sapiens with NA as ligand. Structure known Active Site: AC1. 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 Mon Nov 5 12:51:48 2007
Categories: Homo sapiens | Single protein | Bravo, J. | Cardenes, N. | Deribe, Y.L. | Dikic, I. | Moncalian, G. | Spinola-Amilibia, M. | NA | Adaptor protein | Cd2 associated protein | Coiled coil | Cytoskeletal rearrangements | Egfr downregulation | Phosphorylation | Protein binding | Sh3 | Sh3 domain | Sh3-binding | Signaling protein | Surface active protein
