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4X0C

Crystal structure of P domain from norovirus strain NSW0514 in complex with HBGA type Lex (triglycan)

4X0C の概要
エントリーDOI10.2210/pdb4x0c/pdb
関連するPDBエントリー4OOS 4OP7 4WZT
関連するBIRD辞書のPRD_IDPRD_900120
分子名称VP1, alpha-L-fucopyranose-(1-3)-[beta-D-galactopyranose-(1-4)]2-acetamido-2-deoxy-alpha-D-glucopyranose, 1,2-ETHANEDIOL, ... (5 entities in total)
機能のキーワードviral capsid protein, protruding domain, viral protein
由来する生物種Norovirus Hu/GII.4/Sydney/NSW0514/2012/AU
タンパク質・核酸の鎖数2
化学式量合計69705.32
構造登録者
Singh, B.K.,Hansman, G.S. (登録日: 2014-11-21, 公開日: 2014-12-17, 最終更新日: 2024-01-10)
主引用文献Singh, B.K.,Leuthold, M.M.,Hansman, G.S.
Human noroviruses' fondness for histo-blood group antigens.
J.Virol., 89:2024-2040, 2015
Cited by
PubMed Abstract: Human noroviruses are the dominant cause of outbreaks of gastroenteritis around the world. Human noroviruses interact with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. Indeed, synthetic HBGAs or HBGA-expressing enteric bacteria were shown to enhance norovirus infection in B cells. A number of studies have found a possible relationship between HBGA type and norovirus susceptibility. The genogroup II, genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Here we show high-resolution X-ray crystal structures of the capsid protruding (P) domains from epidemic GII.4 variants from 2004, 2006, and 2012, cocrystallized with a panel of HBGA types (H type 2, Lewis Y, Lewis B, Lewis A, Lewis X, A type, and B type). Many of the HBGA binding interactions were found to be complex, involving capsid loop movements, alternative HBGA conformations, and HBGA rotations. We showed that a loop (residues 391 to 395) was elegantly repositioned to allow for Lewis Y binding. This loop was also slightly shifted to provide direct hydrogen- and water-mediated bonds with Lewis B. We considered that the flexible loop modulated Lewis HBGA binding. The GII.4 noroviruses have dominated outbreaks over the past decade, which may be explained by their exquisite HBGA binding mechanisms, their fondness for Lewis HBGAs, and their temporal amino acid modifications.
PubMed: 25428879
DOI: 10.1128/JVI.02968-14
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.72 Å)
構造検証レポート
Validation report summary of 4x0c
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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