2GRI

NMR Structure of the SARS-CoV non-structural protein nsp3a

2GRI の概要

• エントリーDOI: 10.2210/pdb2gri/pdb
• NMR情報: BMRB: 7019
• 分子名称: NSP3 (1 entity in total)
• 機能のキーワード: sars-cov, non-structural protein, nsp3, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg, viral protein
• 由来する生物種: SARS coronavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12648.01

構造登録者

Serrano, P.,Almeida, M.S.,Johnson, M.A.,Herrmann, T.,Saikatendu, K.S.,Joseph, J.,Subramanian, V.,Neuman, B.W.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (登録日: 2006-04-24, 公開日: 2006-12-19, 最終更新日: 2024-05-08)

主引用文献

Serrano, P.,Johnson, M.A.,Almeida, M.S.,Horst, R.,Herrmann, T.,Joseph, J.S.,Neuman, B.W.,Subramanian, V.,Saikatendu, K.S.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wuthrich, K.
Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.
J.Virol., 81:12049-12060, 2007

PubMed Abstract: This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.

PubMed: 17728234
DOI: 10.1128/JVI.00969-07

実験手法

SOLUTION NMR