1D5F

STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY

1D5F の概要

• エントリーDOI: 10.2210/pdb1d5f/pdb
• 関連するPDBエントリー: 1UBQ
• 分子名称: E6AP HECT CATALYTIC DOMAIN, E3 LIGASE (1 entity in total)
• 機能のキーワード: bilobal structure, elongated shape, e3 ligase, ligase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 124621.30

構造登録者

Huang, L.,Kinnucan, E.,Wang, G.,Beaudenon, S.,Howley, P.M.,Huibregtse, J.M.,Pavletich, N.P. (登録日: 1999-10-07, 公開日: 1999-11-17, 最終更新日: 2024-02-07)

主引用文献

Huang, L.,Kinnucan, E.,Wang, G.,Beaudenon, S.,Howley, P.M.,Huibregtse, J.M.,Pavletich, N.P.
Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade.
Science, 286:1321-1326, 1999

PubMed Abstract: The E6AP ubiquitin-protein ligase (E3) mediates the human papillomavirus-induced degradation of the p53 tumor suppressor in cervical cancer and is mutated in Angelman syndrome, a neurological disorder. The crystal structure of the catalytic hect domain of E6AP reveals a bilobal structure with a broad catalytic cleft at the junction of the two lobes. The cleft consists of conserved residues whose mutation interferes with ubiquitin-thioester bond formation and is the site of Angelman syndrome mutations. The crystal structure of the E6AP hect domain bound to the UbcH7 ubiquitin-conjugating enzyme (E2) reveals the determinants of E2-E3 specificity and provides insights into the transfer of ubiquitin from the E2 to the E3.

PubMed: 10558980
DOI: 10.1126/science.286.5443.1321

実験手法

X-RAY DIFFRACTION (2.8 Å)