5DLM

Complex of Influenza M2e and Antibody


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.189 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of the Conserved Amino Terminus of the Extracellular Domain of Matrix Protein 2 of Influenza A Virus Gripped by an Antibody.

Cho, K.J.Schepens, B.Moonens, K.Deng, L.Fiers, W.Remaut, H.Saelens, X.

(2015) J Virol 90: 611-615

  • DOI: https://doi.org/10.1128/JVI.02105-15
  • Primary Citation of Related Structures:  
    5DLM

  • PubMed Abstract: 

    We report the crystal structure of the M2 ectodomain (M2e) in complex with a monoclonal antibody that binds the amino terminus of M2. M2e extends into the antibody binding site to form an N-terminal β-turn near the bottom of the paratope. This M2e folding differs significantly from that of M2e in complex with an antibody that binds another part of M2e. This suggests that M2e can adopt at least two conformations that can elicit protective antibodies.


  • Organizational Affiliation

    Medical Biotechnology Center, VIB, Ghent, Belgium Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Heavy chain of monoclonal antibodyA [auth H],
C [auth I]
216Mus musculusMutation(s): 0 
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Light chain of monoclonal antibodyB [auth L],
D [auth M]
217Mus musculusMutation(s): 0 
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Matrix protein 2E [auth X],
F [auth Y]
23Influenza A virusMutation(s): 1 
UniProt
Find proteins for P06821 (Influenza A virus (strain A/Puerto Rico/8/1934 H1N1))
Explore P06821 
Go to UniProtKB:  P06821
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06821
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.189 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 92.64α = 90
b = 101.44β = 90
c = 212.49γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Fonds Wetenschappelijk OnderzoekBelgium3G052412N
Fonds Wetenschappelijk Onderzoek - VlaanderenBelgium--
China Scholarship CouncilChina2011674067
VIBBelgiumIUAP BELVIR project p7/45
Ghent UniversityBelgiumBOF12/GOA/014

Revision History  (Full details and data files)

  • Version 1.0: 2015-10-28
    Type: Initial release
  • Version 1.1: 2015-12-30
    Changes: Database references
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Refinement description