4K7D

Crystal Structure of Parkin C-terminal RING domains

4K7D の概要

• エントリーDOI: 10.2210/pdb4k7d/pdb
• 分子名称: E3 ubiquitin-protein ligase parkin, ZINC ION, MALONATE ION, ... (5 entities in total)
• 機能のキーワード: ring domains, zinc fingers, rbr ubiquitin ligase, e3 ubiquitin protein ligase, ubiquitin, ubch7, ligase
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• 細胞内の位置: Nucleus (By similarity): Q9JK66
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 112404.62

構造登録者

Sauve, V.,Trempe, J.-F.,Menade, M.,Gehring, K. (登録日: 2013-04-17, 公開日: 2013-05-15, 最終更新日: 2024-02-28)

主引用文献

Trempe, J.F.,Sauve, V.,Grenier, K.,Seirafi, M.,Tang, M.Y.,Menade, M.,Al-Abdul-Wahid, S.,Krett, J.,Wong, K.,Kozlov, G.,Nagar, B.,Fon, E.A.,Gehring, K.
Structure of parkin reveals mechanisms for ubiquitin ligase activation.
Science, 340:1451-1455, 2013

PubMed Abstract: Mutations in the PARK2 (parkin) gene are responsible for an autosomal recessive form of Parkinson's disease. The parkin protein is a RING-in-between-RING E3 ubiquitin ligase that exhibits low basal activity. We describe the crystal structure of full-length rat parkin. The structure shows parkin in an autoinhibited state and provides insight into how it is activated. RING0 occludes the ubiquitin acceptor site Cys(431) in RING2, whereas a repressor element of parkin binds RING1 and blocks its E2-binding site. Mutations that disrupted these inhibitory interactions activated parkin both in vitro and in cells. Parkin is neuroprotective, and these findings may provide a structural and mechanistic framework for enhancing parkin activity.

PubMed: 23661642
DOI: 10.1126/science.1237908

実験手法

X-RAY DIFFRACTION (2.8 Å)