4CR0

Crystal Structure of H5 (VN1194) Asn186Lys/Gly143Arg Mutant Haemagglutinin

4CR0 の概要

• エントリーDOI: 10.2210/pdb4cr0/pdb
• 関連するPDBエントリー: 4CQP 4CQQ 4CQR 4CQS 4CQT 4CQU 4CQV 4CQW 4CQX 4CQY 4CQZ
• 分子名称: Hemagglutinin HA1, Hemagglutinin HA2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: viral protein, sialic acid, glycoprotein, virus receptor, avian flu, sialyllactosamine, 3sln, 3'sln, 6sln, 6'sln, lsta
• 由来する生物種: Influenza A virus (A/Vietnam/1194/2004(H5N1)); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57038.77

構造登録者

Collins, P.J.,Vachieri, S.G.,Xiong, X.,Xiao, H.,Martin, S.R.,Coombs, P.J.,Liu, J.,Walker, P.A.,Lin, Y.P.,McCauley, J.W.,Gamblin, S.J.,Skehel, J.J. (登録日: 2014-02-21, 公開日: 2014-05-28, 最終更新日: 2024-11-20)

主引用文献

Xiong, X.,Xiao, H.,Martin, S.R.,Coombs, P.J.,Liu, J.,Collins, P.J.,Vachieri, S.G.,Walker, P.A.,Lin, Y.P.,Mccauley, J.W.,Gamblin, S.J.,Skehel, J.J.
Enhanced Human Receptor Binding by H5 Haemagglutinins.
Virology, 456:179-, 2014

PubMed Abstract: Mutant H5N1 influenza viruses have been isolated from humans that have increased human receptor avidity. We have compared the receptor binding properties of these mutants with those of wild-type viruses, and determined the structures of their haemagglutinins in complex with receptor analogues. Mutants from Vietnam bind tighter to human receptor by acquiring basic residues near the receptor binding site. They bind more weakly to avian receptor because they lack specific interactions between Asn-186 and Gln-226. In contrast, a double mutant, Δ133/Ile155Thr, isolated in Egypt has greater avidity for human receptor while retaining wild-type avidity for avian receptor. Despite these increases in human receptor binding, none of the mutants prefers human receptor, unlike aerosol transmissible H5N1 viruses. Nevertheless, mutants with high avidity for both human and avian receptors may be intermediates in the evolution of H5N1 viruses that could infect both humans and poultry.

PubMed: 24889237
DOI: 10.1016/J.VIROL.2014.03.008

実験手法

X-RAY DIFFRACTION (2.65 Å)