2bz8
From Proteopedia
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| - | [[Image:2bz8.gif|left|200px]] | + | [[Image:2bz8.gif|left|200px]] |
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| - | '''N-TERMINAL SH3 DOMAIN OF CIN85 BOUND TO CBL-B PEPTIDE''' | + | {{Structure |
| + | |PDB= 2bz8 |SIZE=350|CAPTION= <scene name='initialview01'>2bz8</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''N-TERMINAL SH3 DOMAIN OF CIN85 BOUND TO CBL-B PEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BZ8 is a [ | + | 2BZ8 is a [[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=2BZ8 OCA]. |
==Reference== | ==Reference== | ||
| - | Cbl promotes clustering of endocytic adaptor proteins., Jozic D, Cardenes N, Deribe YL, Moncalian G, Hoeller D, Groemping Y, Dikic I, Rittinger K, Bravo J, Nat Struct Mol Biol. 2005 Nov;12(11):972-9. PMID:[http:// | + | Cbl promotes clustering of endocytic adaptor proteins., Jozic D, Cardenes N, Deribe YL, Moncalian G, Hoeller D, Groemping Y, Dikic I, Rittinger K, Bravo J, Nat Struct Mol Biol. 2005 Nov;12(11):972-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16228008 16228008] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:42 2008'' |
Revision as of 14:08, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-TERMINAL SH3 DOMAIN OF CIN85 BOUND TO CBL-B PEPTIDE
Overview
The ubiquitin ligases c-Cbl and Cbl-b play a crucial role in receptor downregulation by mediating multiple monoubiquitination of receptors and promoting their sorting for lysosomal degradation. Their function is modulated through interactions with regulatory proteins including CIN85 and PIX, which recognize a proline-arginine motif in Cbl and thus promote or inhibit receptor endocytosis. We report the structures of SH3 domains of CIN85 and beta-PIX in complex with a proline-arginine peptide from Cbl-b. Both structures reveal a heterotrimeric complex containing two SH3 domains held together by a single peptide. Trimerization also occurs in solution and is facilitated by the pseudo-symmetrical peptide sequence. Moreover, ternary complexes of CIN85 and Cbl are formed in vivo and are important for the ability of Cbl to promote epidermal growth factor receptor (EGFR) downregulation. These results provide molecular explanations for a novel mechanism by which Cbl controls receptor downregulation.
About this Structure
2BZ8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Cbl promotes clustering of endocytic adaptor proteins., Jozic D, Cardenes N, Deribe YL, Moncalian G, Hoeller D, Groemping Y, Dikic I, Rittinger K, Bravo J, Nat Struct Mol Biol. 2005 Nov;12(11):972-9. PMID:16228008
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