2KR1

Solution NMR structure of zinc binding N-terminal domain of ubiquitin-protein ligase E3A from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HR3662

2KR1 の概要

• エントリーDOI: 10.2210/pdb2kr1/pdb
• NMR情報: BMRB: 16620
• 分子名称: Ubiquitin protein ligase E3A, ZINC ION (2 entities in total)
• 機能のキーワード: ligase, ubl conjugation pathway, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, structural genomics consortium (sgc)
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9477.12

構造登録者

Lemak, A.,Yee, A.,Fares, C.,Semesi, A.,Xiao, R.,Montelione, G.,Dhe-Paganon, S.,Arrowsmith, C.,Northeast Structural Genomics Consortium (NESG),Structural Genomics Consortium (SGC) (登録日: 2009-11-27, 公開日: 2009-12-22, 最終更新日: 2024-11-06)

主引用文献

Lemak, A.,Yee, A.,Bezsonova, I.,Dhe-Paganon, S.,Arrowsmith, C.H.
Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A.
J.Biomol.Nmr, 51:185-190, 2011

PubMed Abstract: Ube3A (also referred to as E6AP for E6 Associated Protein) is a E3 ubiquitin-protein ligase implicated in the development of Angelman syndrome by controlling degradation of synaptic protein Arc and oncogenic papilloma virus infection by controlling degradation of p53. This article describe the solution NMR structure of the conserved N-terminal domain of human Ube3A (residues 24-87) that contains two residues (Cys44 and Arg62) found to be mutated in patients with Angelman syndrome. The structure of this domain adopts a novel Zn-binding fold we called AZUL (Amino-terminal Zn-finger of Ube3a Ligase). The AZUL domain has a helix-loop-helix architecture with a Zn ion coordinated by four Cys residues arranged in Cys-X(4)-Cys-X(4)-Cys-X(28)-Cys motif. Three of the Zn-bound residues are located in a 23-residue long and well structured loop that connects two α-helicies.

PubMed: 21947926
DOI: 10.1007/s10858-011-9552-y

実験手法

SOLUTION NMR