2B4I

Crystal Structure of the Rhesus Rotavirus VP5 Antigen Domain Trimer

2B4I の概要

• エントリーDOI: 10.2210/pdb2b4i/pdb
• 関連するPDBエントリー: 1SLQ 2B4H
• 分子名称: Outer capsid protein VP4 (2 entities in total)
• 機能のキーワード: beta sandwich; greek key; membrane penetration protein; non-enveloped virus; spike protein; rearrangement, viral protein
• 由来する生物種: Rhesus rotavirus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 85574.31

構造登録者

Yoder, J.D.,Dormitzer, P.R. (登録日: 2005-09-24, 公開日: 2006-04-18, 最終更新日: 2023-08-23)

主引用文献

Yoder, J.D.,Dormitzer, P.R.
Alternative intermolecular contacts underlie the rotavirus VP5(*) two- to three-fold rearrangement
Embo J., 25:1559-1568, 2006

PubMed Abstract: The spike protein VP4 is a key component of the membrane penetration apparatus of rotavirus, a nonenveloped virus that causes childhood gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a potential membrane interaction region, and primes rotavirus for cell entry. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. Here, we report that a globular domain of VP5*, the VP5* antigen domain, is an autonomously folding unit that alternatively forms well-ordered dimers and trimers. Because the domain contains heterotypic neutralizing epitopes and is soluble when expressed directly, it is a promising potential subunit vaccine component. X-ray crystal structures show that the dimer resembles the spike body on trypsin-primed virions, and the trimer resembles the folded-back form of the spike. The same structural elements pack differently to form key intermolecular contacts in both oligomers. The intrinsic molecular property of alternatively forming dimers and trimers facilitates the VP5* reorganization, which is thought to mediate membrane penetration during cell entry.

PubMed: 16511559
DOI: 10.1038/sj.emboj.7601034

実験手法

X-RAY DIFFRACTION (2 Å)