2j6k
From Proteopedia
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|PDB= 2j6k |SIZE=350|CAPTION= <scene name='initialview01'>2j6k</scene>, resolution 2.775Å | |PDB= 2j6k |SIZE=350|CAPTION= <scene name='initialview01'>2j6k</scene>, resolution 2.775Å | ||
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6k OCA], [http://www.ebi.ac.uk/pdbsum/2j6k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j6k RCSB]</span> | ||
}} | }} | ||
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[[Category: Moncalian, G.]] | [[Category: Moncalian, G.]] | ||
[[Category: Spinola-Amilibia, M.]] | [[Category: Spinola-Amilibia, M.]] | ||
| - | [[Category: NA]] | ||
[[Category: adaptor protein]] | [[Category: adaptor protein]] | ||
[[Category: cd2 associated protein]] | [[Category: cd2 associated protein]] | ||
| Line 42: | Line 44: | ||
[[Category: surface active protein]] | [[Category: surface active protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:43 2008'' |
Revision as of 00:53, 31 March 2008
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| , resolution 2.775Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 31 03:53:43 2008
Categories: Homo sapiens | Single protein | Bravo, J. | Cardenes, N. | Deribe, Y L. | Dikic, I. | Moncalian, G. | Spinola-Amilibia, M. | Adaptor protein | Cd2 associated protein | Coiled coil | Cytoskeletal rearrangement | Egfr downregulation | Phosphorylation | Protein binding | Sh3 | Sh3 domain | Sh3-binding | Signaling protein | Surface active protein
