1EW3

CRYSTAL STRUCTURE OF THE MAJOR HORSE ALLERGEN EQU C 1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.195 

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This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes.

Lascombe, M.B.Gregoire, C.Poncet, P.Tavares, G.A.Rosinski-Chupin, I.Rabillon, J.Goubran-Botros, H.Mazie, J.C.David, B.Alzari, P.M.

(2000) J Biol Chem 275: 21572-21577

  • DOI: https://doi.org/10.1074/jbc.M002854200
  • Primary Citation of Related Structures:  
    1EW3

  • PubMed Abstract: 

    The three-dimensional structure of the major horse allergen Equ c 1 has been determined at 2.3 A resolution by x-ray crystallography. Equ c 1 displays the typical fold of lipocalins, a beta-barrel flanked by a C-terminal alpha-helix. The space between the two beta-sheets of the barrel defines an internal cavity that could serve, as in other lipocalins, for the binding and transport of small hydrophobic ligands. Equ c 1 crystallizes in a novel dimeric form, which is distinct from that observed in other lipocalin dimers and corresponds to the functional form of the allergen. Binding studies of point mutants of the allergen with specific monoclonal antibodies raised in mouse and IgE serum from horse allergic patients allowed to identify putative B cell antigenic determinants. In addition, total inhibition of IgE serum recognition by a single specific monoclonal antibody revealed the restricted nature of the IgE binding target on the molecular surface of Equ c 1.


  • Organizational Affiliation

    Unité de Biochimie Structurale (CNRS URA 2185), Unité d'Immuno-Allergie, 25 et 28 rue du Docteur Roux, 75724 Paris Cedex 15, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ALLERGEN EQU C 1159Equus caballusMutation(s): 0 
UniProt
Find proteins for Q95182 (Equus caballus)
Explore Q95182 
Go to UniProtKB:  Q95182
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ95182
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.195 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.04α = 90
b = 84.04β = 90
c = 58.48γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
REFMACrefinement

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2000-05-03
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance