2A2G

THE CRYSTAL STRUCTURES OF A2U-GLOBULIN AND ITS COMPLEX WITH A HYALINE DROPLET INDUCER.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.248 
  • R-Value Observed: 0.248 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The structures of alpha 2u-globulin and its complex with a hyaline droplet inducer.

Chaudhuri, B.N.Kleywegt, G.J.Bjorkman, J.Lehman-McKeeman, L.D.Oliver, J.D.Jones, T.A.

(1999) Acta Crystallogr D Biol Crystallogr 55: 753-762

  • DOI: https://doi.org/10.1107/s0907444998017211
  • Primary Citation of Related Structures:  
    2A2G, 2A2U

  • PubMed Abstract: 

    Alpha 2u-globulin (A2U) is the major urinary protein excreted by adult male rats. The structure of a monoclinic crystal form of A2U was reported in 1992 [Böcskei et al. (1992). Nature (London), 360, 186-188]. The structures of an orthorhombic crystal form of A2U at 2. 5 A resolution (refined to an R factor of 0.248; Rfree = 0.264) and of a complex between A2U and d-limonene 1,2-epoxide (DLO) at 2.9 A resolution (R factor = 0.248; Rfree = 0.260) are presented here. DLO is one of a diverse group of chemicals which cause a male rat-specific renal carcinogenesis called hyaline-droplet nephropathy. The rate-determining step in the development of this disorder is the binding of the toxin to A2U. Comparison of the cavities in A2U and in the corresponding mouse urinary protein (MUP) reveal that the former is tailor-made for small oval hydrophobic ligands such as DLO. The cavity in MUP is more shallow and elongated and cannot easily accommodate such ligands.


  • Organizational Affiliation

    Department of Cell and Molecular Biology, Uppsala University, Biomedical Centre, Box 590, SE-751 24 Uppsala, Sweden.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (ALPHA-2U-GLOBULIN)
A, B, C, D
181Rattus norvegicusMutation(s): 0 
UniProt
Find proteins for P02761 (Rattus norvegicus)
Explore P02761 
Go to UniProtKB:  P02761
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02761
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.248 
  • R-Value Observed: 0.248 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.81α = 90
b = 98.01β = 90
c = 123.37γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALAdata scaling
AMoREphasing
CNSrefinement
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-08-13
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations, Structure summary