2bz8
From Proteopedia
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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 with as ligand. Known structural/functional Site: . 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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