1FBV

STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES

1FBV の概要

• エントリーDOI: 10.2210/pdb1fbv/pdb
• 分子名称: SIGNAL TRANSDUCTION PROTEIN CBL, ZAP-70 PEPTIDE, UBIQUITIN-CONJUGATING ENZYME E12-18 KDA UBCH7, ... (5 entities in total)
• 機能のキーワード: cbl, ubch7, zap-70, e2, ubiquitin, e3, phosphorylation, tyrosine kinase, ubiquitination, protein degradation, ligase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P22681; Nucleus : P68036
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 64330.24

構造登録者

Zheng, N.,Wang, P.,Jeffrey, P.D.,Pavletich, N.P. (登録日: 2000-07-17, 公開日: 2000-08-30, 最終更新日: 2024-10-30)

主引用文献

Zheng, N.,Wang, P.,Jeffrey, P.D.,Pavletich, N.P.
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.
Cell(Cambridge,Mass.), 102:533-539, 2000

PubMed Abstract: 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.

PubMed: 10966114
DOI: 10.1016/S0092-8674(00)00057-X

実験手法

X-RAY DIFFRACTION (2.9 Å)