4JU0
Crystal structure of 2009 pandemic influenza virus hemagglutinin mutant D225E complexed with human receptor analogue LSTc
4JU0 の概要
| エントリーDOI | 10.2210/pdb4ju0/pdb |
| 関連するPDBエントリー | 4JTV 4JTX 4JUG 4JUH 4JUJ |
| 分子名称 | Hemagglutinin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| 機能のキーワード | virus attachment, membrane fusion, viral protein |
| 由来する生物種 | Influenza A virus 詳細 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 333887.93 |
| 構造登録者 | |
| 主引用文献 | Zhang, W.,Shi, Y.,Qi, J.,Gao, F.,Li, Q.,Fan, Z.,Yan, J.,Gao, G.F. Molecular basis of the receptor binding specificity switch of the hemagglutinins from both the 1918 and 2009 pandemic influenza A viruses by a D225G substitution J.Virol., 87:5949-5958, 2013 Cited by PubMed Abstract: Influenza A virus uses sialic acids as cell entry receptors, and there are two main receptor forms, α2,6 linkage or α2,3 linkage to galactose, that determine virus host ranges (mammalian or avian). The receptor binding hemagglutinins (HAs) of both 1918 and 2009 pandemic H1N1 (18H1 and 09H1, respectively) influenza A viruses preferentially bind to the human α2,6 linkage receptor. A single D225G mutation in both H1s switches receptor binding specificity from α2,6 linkage binding to dual receptor binding. However, the molecular basis for this specificity switch is not fully understood. Here, we show via H1-ligand complex structures that the D225G substitution results in a loss of a salt bridge between amino acids D225 and K222, enabling the key residue Q226 to interact with the avian receptor, thereby obtaining dual receptor binding. This is further confirmed by a D225E mutant that retains human receptor binding specificity with the salt bridge intact. PubMed: 23514882DOI: 10.1128/JVI.00545-13 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.908 Å) |
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