4WE9

The crystal structure of hemagglutinin from influenza virus A/Victoria/361/2011 in complex with 3'SLN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 

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Literature

Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins.

Yang, H., Carney, P.J., Chang, J.C., Guo, Z., Villanueva, J.M., Stevens, J.

(2015) Virology 477C: 18-31

  • DOI: https://doi.org/10.1016/j.virol.2014.12.024
  • Primary Citation of Related Structures:  
    4WE4, 4WE5, 4WE6, 4WE7, 4WE8, 4WE9, 4WEA

  • PubMed Abstract: 

    A(H3N2) influenza viruses have circulated in humans since 1968, and antigenic drift of the hemagglutinin (HA) protein continues to be a driving force that allows the virus to escape the human immune response. Since the major antigenic sites of the HA overlap into the receptor binding site (RBS) of the molecule, the virus constantly struggles to effectively adapt to host immune responses, without compromising its functionality. Here, we have structurally assessed the evolution of the A(H3N2) virus HA RBS, using an established recombinant expression system. Glycan binding specificities of nineteen A(H3N2) influenza virus HAs, each a component of the seasonal influenza vaccine between 1968 and 2012, were analyzed. Results suggest that while its receptor-binding site has evolved from one that can bind a broad range of human receptor analogs to one with a more restricted binding profile for longer glycans, the virus continues to circulate and transmit efficiently among humans.

    • Organizational Affiliation: 

    Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hemagglutinin515Influenza A virus (A/Victoria/361/2011(H3N2))Mutation(s): 0 
Gene Names: HA
UniProt
Find proteins for R9U684 (Influenza A virus)
Explore R9U684 
Go to UniProtKB:  R9U684
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupR9U684
Glycosylation
Glycosylation Sites: 8
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

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Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
B
2N-Glycosylation
Glycosylation Resources
GlyTouCan:  G42666HT
GlyCosmos:  G42666HT
GlyGen:  G42666HT
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.141α = 90
b = 101.141β = 90
c = 384.931γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-02-11
    Type: Initial release
  • Version 2.0: 2017-09-27
    Changes: Atomic model, Data collection, Database references, Derived calculations, Other, Source and taxonomy, Structure summary
  • Version 3.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Atomic model, Data collection, Derived calculations, Refinement description, Structure summary
  • Version 3.1: 2023-12-27
    Changes: Data collection, Database references, Structure summary