2FXP

Solution Structure of the SARS-Coronavirus HR2 Domain

2FXP の概要

• エントリーDOI: 10.2210/pdb2fxp/pdb
• NMR情報: BMRB: 6969
• 分子名称: Spike glycoprotein (1 entity in total)
• 機能のキーワード: prefusion intermediate, trimer, coiled-coil, viral protein
• 由来する生物種: SARS coronavirus
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein: P59594
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 18272.15

構造登録者

Caffrey, M.,Hakansson-McReynolds, S.,Jiang, S. (登録日: 2006-02-06, 公開日: 2006-03-07, 最終更新日: 2024-05-29)

主引用文献

Hakansson-McReynolds, S.,Jiang, S.,Rong, L.,Caffrey, M.
Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state
J.Biol.Chem., 281:11965-11971, 2006

PubMed Abstract: The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS.

PubMed: 16507566
DOI: 10.1074/jbc.M601174200

実験手法

SOLUTION NMR