2VIT

INFLUENZA VIRUS HEMAGGLUTININ, MUTANT WITH THR 155 REPLACED BY ILE, COMPLEXED WITH A NEUTRALIZING ANTIBODY

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.25 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Antigen distortion allows influenza virus to escape neutralization.

Fleury, D., Wharton, S.A., Skehel, J.J., Knossow, M., Bizebard, T.

(1998) Nat Struct Biol 5: 119-123

  • DOI: https://doi.org/10.1038/nsb0298-119
  • Primary Citation of Related Structures:  
    2VIR, 2VIS, 2VIT, 2VIU

  • PubMed Abstract: 

    The structure of the hemagglutinin (HA) of a mutant influenza virus that escapes neutralization by a monoclonal antibody shows that the mutation causes changes in HA structure which avoid an energetically less favorable conformation. However, the structure of the mutant HA.Fab complex indicates that the antibody binds selectively to mutant HA in a wild type-like distorted conformation. The association of an antibody with a less favored HA conformation represents an alternative to previously described mechanisms of escape from neutralization by antibodies.

    • Organizational Affiliation: 

    Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Gif-sur-Yvette, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
IMMUNOGLOBULIN (IGG1, LAMBDA)210Mus musculusMutation(s): 0 
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
IMMUNOGLOBULIN (IGG1, LAMBDA)221Mus musculusMutation(s): 0 
UniProt
Find proteins for Q99LC4 (Mus musculus)
Explore Q99LC4 
Go to UniProtKB:  Q99LC4
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UniProt GroupQ99LC4
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
HEMAGGLUTININ282Influenza A virus (A/X-31(H3N2))Mutation(s): 4 
UniProt
Find proteins for P03437 (Influenza A virus (strain A/Aichi/2/1968 H3N2))
Explore P03437 
Go to UniProtKB:  P03437
Entity Groups  
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UniProt GroupP03437
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.25 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.188 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.5α = 90
b = 85.5β = 90
c = 515γ = 120
Software Package:
Software NamePurpose
HKLdata collection
X-PLORmodel building
X-PLORrefinement
HKLdata reduction
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-04-29
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Data collection, Database references, Derived calculations, Other
  • Version 1.4: 2024-11-20
    Changes: Data collection, Structure summary