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4CQS

H5 (VN1194) Asn186Lys Mutant Haemagglutinin in Complex with Avian Receptor Analogue 3'SLN

4CQS の概要
エントリーDOI10.2210/pdb4cqs/pdb
関連するPDBエントリー4CQP 4CQQ 4CQR 4CQT 4CQU 4CQV 4CQW 4CQX 4CQY 4CQZ 4CR0
分子名称Hemagglutinin HA1, Hemagglutinin HA2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 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58846.54
構造登録者
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.55 Å)
構造検証レポート
Validation report summary of 4cqs
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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