3LQ6

Crystal Structure of Murine Norovirus Protruding (P) Domain

3LQ6 の概要

• エントリーDOI: 10.2210/pdb3lq6/pdb
• 関連するPDBエントリー: 3LQE
• 分子名称: Capsid protein (2 entities in total)
• 機能のキーワード: viral capsid protein, protruding (p) domain, viral protein
• 由来する生物種: Murine norovirus 1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69716.56

構造登録者

Rubin, J.R.,Stuckey, J.A. (登録日: 2010-02-08, 公開日: 2010-04-21, 最終更新日: 2023-09-06)

主引用文献

Taube, S.,Rubin, J.R.,Katpally, U.,Smith, T.J.,Kendall, A.,Stuckey, J.A.,Wobus, C.E.
High-resolution x-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain.
J.Virol., 84:5695-5705, 2010

PubMed Abstract: Murine noroviruses (MNV) are closely related to the human noroviruses (HuNoV), which cause the majority of nonbacterial gastroenteritis. Unlike HuNoV, MNV grow in culture and in a small-animal model that represents a tractable model to study norovirus biology. To begin a detailed investigation of molecular events that occur during norovirus binding to cells, the crystallographic structure of the murine norovirus 1 (MNV-1) capsid protein protruding (P) domain has been determined. Crystallization of the bacterially expressed protein yielded two different crystal forms (Protein Data Bank identifiers [PDB ID], 3LQ6 and 3LQE). Comparison of the structures indicated a large degree of structural mobility in loops on the surface of the P2 subdomain. Specifically, the A'-B' and E'-F' loops were found in open and closed conformations. These regions of high mobility include the known escape mutation site for the neutralizing antibody A6.2 and an attenuation mutation site, which arose after serial passaging in culture and led to a loss in lethality in STAT1(-/-) mice, respectively. Modeling of a Fab fragment and crystal structures of the P dimer into the cryoelectron microscopy three-dimensional (3D) image reconstruction of the A6.2/MNV-1 complex indicated that the closed conformation is most likely bound to the Fab fragment and that the antibody contact is localized to the A'-B' and E'-F' loops. Therefore, we hypothesize that these loop regions and the flexibility of the P domains play important roles during MNV-1 binding to the cell surface.

PubMed: 20335262
DOI: 10.1128/JVI.00316-10

実験手法

X-RAY DIFFRACTION (2 Å)