4cqs | pdb_00004cqs

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

spinqualitylabelsall models 4cqs, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cqs is a 2 chain structure with sequence from Influenza a virus (a/vietnam/1194/2004(h5n1)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, MPO, NAG, MAN Related: 4cqp, 4cqq, 4cqr, 4cqt, 4cqu, 4cqv, 4cqw, 4cqx, 4cqy, 4cqz, 4cr0 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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, Delta133/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. Enhanced human receptor binding by H5 haemagglutinins.,Xiong X, Xiao H, Martin SR, Coombs PJ, Liu J, Collins PJ, Vachieri SG, Walker PA, Lin YP, McCauley JW, Gamblin SJ, Skehel JJ Virology. 2014 May;456-457:179-87. doi: 10.1016/j.virol.2014.03.008. Epub 2014, Apr 12. PMID:24889237 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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