1fbv
From Proteopedia
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STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES
Overview
Ubiquitin-protein ligases (E3s) regulate diverse cellular processes by, mediating protein ubiquitination. The c-Cbl proto-oncogene is a RING, family E3 that recognizes activated receptor tyrosine kinases, promotes, their ubiquitination by a ubiquitin-conjugating enzyme (E2) and terminates, signaling. The crystal structure of c-Cbl bound to a cognate E2 and a, kinase peptide shows how the RING domain recruits the E2. A comparison, with a HECT family E3-E2 complex indicates that a common E2 motif is, recognized by the two E3 families. The structure reveals a rigid coupling, between the peptide binding and the E2 binding domains and a conserved, surface channel leading from the peptide to the E2 active site, suggesting, that RING E3s may function as scaffolds that position the substrate and, the E2 optimally for ubiquitin transfer.
About this Structure
1FBV is a Protein complex structure of sequences from Homo sapiens with ZN and SO4 as ligands. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases., Zheng N, Wang P, Jeffrey PD, Pavletich NP, Cell. 2000 Aug 18;102(4):533-9. PMID:10966114
Page seeded by OCA on Mon Nov 12 16:51:09 2007
Categories: Homo sapiens | Protein complex | Ubiquitin--protein ligase | Jeffrey, P.D. | Pavletich, N.P. | Wang, P. | Zheng, N. | SO4 | ZN | Cbl | E2 | E3 | Phosphorylation | Protein degradation | Tyrosine kinase | Ubch7 | Ubiquitin | Ubiquitination | Zap-70
