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6BKS

Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin D190E mutant in complex with 6'-SLN

Summary for 6BKS
Entry DOI10.2210/pdb6bks/pdb
DescriptorHemagglutinin, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsinfluenza, hemagglutinin, receptor, viral protein
Biological sourceInfluenza A virus (A/Wyoming/3e/2003(H3))
More
Total number of polymer chains2
Total formula weight59468.98
Authors
Wu, N.C.,Wilson, I.A. (deposition date: 2017-11-09, release date: 2018-02-28, Last modification date: 2024-10-30)
Primary citationWu, N.C.,Thompson, A.J.,Xie, J.,Lin, C.W.,Nycholat, C.M.,Zhu, X.,Lerner, R.A.,Paulson, J.C.,Wilson, I.A.
A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site.
Nat Commun, 9:1264-1264, 2018
Cited by
PubMed Abstract: The hemagglutinin (HA) receptor-binding site (RBS) in human influenza A viruses is critical for attachment to host cells, which imposes a functional constraint on its natural evolution. On the other hand, being part of the major antigenic sites, the HA RBS of human H3N2 viruses needs to constantly mutate to evade the immune system. From large-scale mutagenesis experiments, we here show that several of the natural RBS substitutions become integrated into an extensive epistatic network that prevents substitution reversion. X-ray structural analysis reveals the mechanistic consequences as well as changes in the mode of receptor binding. Further studies are necessary to elucidate whether such entrenchment limits future options for immune escape or adversely affect long-term viral fitness.
PubMed: 29593268
DOI: 10.1038/s41467-018-03663-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

226707

數據於2024-10-30公開中

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