1BJ7

BOVINE LIPOCALIN ALLERGEN BOS D 2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2.

Rouvinen, J.Rautiainen, J.Virtanen, T.Zeiler, T.Kauppinen, J.Taivainen, A.Mantyjarvi, R.

(1999) J Biol Chem 274: 2337-2343

  • DOI: https://doi.org/10.1074/jbc.274.4.2337
  • Primary Citation of Related Structures:  
    1BJ7

  • PubMed Abstract: 

    The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core suitable for ligand binding, and it is possible that Glu115 and Asn37 inside the core are able to make hydrogen bonds with the ligand. Many allergens from different animals belong to the lipocalin family. The amino acid residue similarities between these lipocalins indicate putative regions for IgE binding. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical.


  • Organizational Affiliation

    Department of Chemistry, University of Joensuu, POB 111, FIN-80101 Joensuu, Finland. juha.rouvinen@joensuu.fi


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
D 2156Bos taurusMutation(s): 0 
UniProt
Find proteins for Q28133 (Bos taurus)
Explore Q28133 
Go to UniProtKB:  Q28133
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ28133
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.184 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37α = 90
b = 55.6β = 90
c = 77.2γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 1999-05-11 
  • Deposition Author(s): Rouvinen, J.

Revision History  (Full details and data files)

  • Version 1.0: 1999-05-11
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-02
    Changes: Database references, Refinement description