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4CR0

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

Summary for 4CR0
Entry DOI10.2210/pdb4cr0/pdb
Related4CQP 4CQQ 4CQR 4CQS 4CQT 4CQU 4CQV 4CQW 4CQX 4CQY 4CQZ
DescriptorHemagglutinin HA1, Hemagglutinin HA2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsviral protein, sialic acid, glycoprotein, virus receptor, avian flu, sialyllactosamine, 3sln, 3'sln, 6sln, 6'sln, lsta
Biological sourceInfluenza A virus (A/Vietnam/1194/2004(H5N1))
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Total number of polymer chains2
Total formula weight57038.77
Authors
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. (deposition date: 2014-02-21, release date: 2014-05-28, Last modification date: 2023-12-20)
Primary citationXiong, 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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

226707

數據於2024-10-30公開中

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