2j6o
From Proteopedia
(New page: 200px<br /> <applet load="2j6o" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j6o, resolution 2.225Å" /> '''ATYPICAL POLYPROLI...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2j6o.gif|left|200px]]<br /> | + | [[Image:2j6o.gif|left|200px]]<br /><applet load="2j6o" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2j6o" size=" | + | |
caption="2j6o, resolution 2.225Å" /> | caption="2j6o, resolution 2.225Å" /> | ||
'''ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3 DOMAIN. CMS:CD2 HETEROTRIMER'''<br /> | '''ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3 DOMAIN. CMS:CD2 HETEROTRIMER'''<br /> | ||
==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== | ||
| - | 2J6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2J6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6O OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 15: | ||
[[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.]] | ||
| Line 31: | Line 30: | ||
[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:47 2008'' |
Revision as of 15:59, 21 February 2008
|
ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3 DOMAIN. CMS:CD2 HETEROTRIMER
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
2J6O 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 17:59:47 2008
Categories: Homo sapiens | Protein complex | Bravo, J. | Cardenes, N. | Deribe, Y L. | Dikic, I. | Moncalian, G. | Spinola-Amilibia, M. | Adaptor protein | Cms | Coiled coil | Egfr downregulation | Phosphorylation | Protein binding | Sh3 domain | Sh3 domain recognition | Sh3-binding | Signaling protein
