5CB7

Crystallographic structure of human rotavirus K8 VP8* in complex with A-type HBGA

5CB7 の概要

• エントリーDOI: 10.2210/pdb5cb7/pdb
• 分子名称: Outer capsid protein VP4, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]alpha-D-galactopyranose, 2-acetamido-2-deoxy-alpha-D-galactopyranose, ... (8 entities in total)
• 機能のキーワード: carbohydrate-recognizing protein, lectin, rotavirus, vp8*, viral protein, sugar binding protein
• 由来する生物種: Rotavirus A (strain Human/Japan/K8/1977 G1-P3A[9]-Ix-Rx-Cx-Mx-A1-Nx-Tx-Ex-H3) (RV-A)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38638.26

構造登録者

Yu, X.,Blanchard, H. (登録日: 2015-06-30, 公開日: 2016-06-08, 最終更新日: 2024-03-06)

主引用文献

Yu, X.,Mishra, R.,Holloway, G.,von Itzstein, M.,Coulson, B.S.,Blanchard, H.
Substantial Receptor-induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross-Species Infection.
Chembiochem, 16:2176-2181, 2015

PubMed Abstract: Rotavirus-cell binding is the essential first step in rotavirus infection. This binding is a major determinant of rotavirus tropism, as host cell invasion is necessary to initiate infection. Initial rotavirus-cell interactions are mediated by carbohydrate-recognizing domain VP8* of the rotavirus capsid spike protein VP4. Here, we report the first observation of significant structural rearrangement of VP8* from human and animal rotavirus strains upon glycan receptor binding. The structural adaptability of rotavirus VP8* delivers important insights into how human and animal rotaviruses utilize the wider range of cellular glycans identified as VP8* binding partners. Furthermore, our studies on rotaviruses with atypical genetic makeup provide information expected to be critical for understanding the mechanisms of animal rotavirus gene emergence in humans and support implementation of epidemiologic surveillance of animal reservoirs as well as future vaccination schemes.

PubMed: 26250751
DOI: 10.1002/cbic.201500360

実験手法

X-RAY DIFFRACTION (1.35 Å)