1IHM

CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID

1IHM の概要

• エントリーDOI: 10.2210/pdb1ihm/pdb
• 分子名称: capsid protein (1 entity in total)
• 機能のキーワード: beta-barrel, ef-tu-like domain caliciviridae, t=3 icosahedral capsid, icosahedral virus, virus
• 由来する生物種: Norwalk virus
• 細胞内の位置: Virion: Q83884
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 169889.48

構造登録者

Prasad, B.V.,Hardy, M.E.,Dokland, T.,Bella, J.,Rossmann, M.G.,Estes, M.K. (登録日: 2001-04-19, 公開日: 2001-05-16, 最終更新日: 2024-04-03)

主引用文献

Prasad, B.V.,Hardy, M.E.,Dokland, T.,Bella, J.,Rossmann, M.G.,Estes, M.K.
X-ray crystallographic structure of the Norwalk virus capsid
Science, 286:287-290, 1999

PubMed Abstract: Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded beta-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor-Tu. This subdomain, located at the exterior of the capsid, has the largest sequence variation among Norwalk-like human caliciviruses and is likely to contain the determinants of strain specificity and cell binding.

PubMed: 10514371
DOI: 10.1126/science.286.5438.287

実験手法

X-RAY DIFFRACTION (3.4 Å)