4CQW
H5 (tyTy) Del133/Ile155Thr Mutant Haemagglutinin in Complex with Avian Receptor Analogue 3'SLN
Summary for 4CQW
| Entry DOI | 10.2210/pdb4cqw/pdb |
| Related | 4CQP 4CQQ 4CQR 4CQS 4CQT 4CQU 4CQV 4CQX 4CQY 4CQZ 4CR0 |
| Related PRD ID | PRD_900067 |
| Descriptor | HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | viral protein, haemagglutinin, sialic acid, glycoprotein, virus receptor, avian flu, sialyllactosamine, 3sln, 3'sln, 6sln, 6'sln, lsta |
| Biological source | INFLUENZA A VIRUS (A/TURKEY/TURKEY/1/2005(H5N1)) More |
| Total number of polymer chains | 6 |
| Total formula weight | 172519.68 |
| Authors | 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. (deposition date: 2014-02-21, release date: 2014-05-28, Last modification date: 2024-10-16) |
| Primary citation | 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: 24889237DOI: 10.1016/J.VIROL.2014.03.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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