1LAT

GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.195 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex.

Gewirth, D.T.Sigler, P.B.

(1995) Nat Struct Biol 2: 386-394

  • DOI: https://doi.org/10.1038/nsb0595-386
  • Primary Citation of Related Structures:  
    1LAT

  • PubMed Abstract: 

    Steroid receptors recognize bipartite targets composed of six base-pair half-sites. There are two canonical types of half-site which differ only in their central two base pairs. The crystal structure of an estrogen receptor-like DNA-binding domain bound to the wrong type of half-site (a glucocorticoid response element) reveals an interface that resembles the specific interfaces of the glucocorticoid receptor or estrogen receptor bound to their correct response elements. The underlying stereochemical defect that weakens the non-cognate interface is a difference in the helical geometry of the incorrect DNA half-site which prevents a side-chain contact and results in a gap which is filled by at least five additional fixed water sites, imposing a potential entropic burden on the stability of the interface.


  • Organizational Affiliation

    Department of Molecular Biophysics and Biochemistry, Yale University New Haven, Connecticut 06510, USA.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
GLUCOCORTICOID RECEPTORC [auth A],
D [auth B]
82Rattus norvegicusMutation(s): 8 
Gene Names: Nr3c1Grl
UniProt
Find proteins for P06536 (Rattus norvegicus)
Explore P06536 
Go to UniProtKB:  P06536
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06536
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
DNA (5'-D(*TP*TP*CP*CP*AP*GP*AP*AP*CP*AP*TP*GP*TP*TP*CP*TP*G P*GP*A)-3')A [auth C],
B [auth D]
19N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.195 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.72α = 90
b = 76.07β = 90
c = 118.88γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-04-03
    Type: Initial release
  • Version 1.1: 2008-05-22
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2012-05-23
    Changes: Structure summary
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations