PDBsum entry 3ubj

Viral protein/immune system

PDB id: 3ubj

Contents

Protein chains

(+ 0 more) 323 a.a.

(+ 0 more) 169 a.a.

Ligands

NAG-NAG ×3

GAL-SIA ×4

NAG ×12

Waters ×783

PDB id:

3ubj

Name:

Viral protein/immune system

Title:

Influenza hemagglutinin from the 2009 pandemic in complex with ligand lsta

Structure:

Hemagglutinin ha1. Chain: a, c, e, g, i, k. Fragment: ectodomain ha1, residues 18-344. Engineered: yes. Mutation: yes. Hemagglutinin ha2. Chain: b, d, f, h, j, l. Fragment: ectodomain ha2, residues 345-520. Engineered: yes

Source:

Influenza a virus. Organism_taxid: 641501. Strain: sw1 a/california/04/2009. Gene: ha, hemagglutinin. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Resolution:

2.25Å R-factor: 0.204 R-free: 0.252

Authors:

R.Xu,I.A.Wilson

Key ref:

R.Xu et al. (2012). Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic. J Virol, 86, 982-990. PubMed id: 22072785

Date:

24-Oct-11 Release date: 23-Nov-11

Protein chains

C3W5S1  (C3W5S1_I09A0) -  Hemagglutinin from Influenza A virus (strain swl A/California/04/2009 H1N1)

Seq: 566 a.a.

Struc: 323 a.a.*

Protein chains

C3W5S1  (C3W5S1_I09A0) -  Hemagglutinin from Influenza A virus (strain swl A/California/04/2009 H1N1)

Seq: 566 a.a.

Struc: 169 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

J Virol 86:982-990 (2012)

PubMed id: 22072785

Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic.

R.Xu, R.McBride, C.M.Nycholat, J.C.Paulson, I.A.Wilson.

ABSTRACT

Influenza virus hemagglutinin (HA) is the viral envelope protein that mediates viral attachment to host cells and elicits membrane fusion. The HA receptor-binding specificity is a key determinant for the host range and transmissibility of influenza viruses. In human pandemics of the 20th century, the HA normally has acquired specificity for human-like receptors before widespread infection. Crystal structures of the H1 HA from the 2009 human pandemic (A/California/04/2009 [CA04]) in complex with human and avian receptor analogs reveal conserved recognition of the terminal sialic acid of the glycan ligands. However, favorable interactions beyond the sialic acid are found only for α2-6-linked glycans and are mediated by Asp190 and Asp225, which hydrogen bond with Gal-2 and GlcNAc-3. For α2-3-linked glycan receptors, no specific interactions beyond the terminal sialic acid are observed. Our structural and glycan microarray analyses, in the context of other high-resolution HA structures with α2-6- and α2-3-linked glycans, now elucidate the structural basis of receptor-binding specificity for H1 HAs in human and avian viruses and provide a structural explanation for the preference for α2-6 siaylated glycan receptors for the 2009 pandemic swine flu virus.