Document Detail


Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains.
MedLine Citation:
PMID:  10882070     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The crystal structure of a heterodimer between the ligand-binding domains (LBDs) of the human RARalpha bound to a selective antagonist and the constitutively active mouse RXRalphaF318A mutant shows that, pushed by a bulky extension of the ligand, RARalpha helix H12 adopts an antagonist position. The unexpected presence of a fatty acid in the ligand-binding pocket of RXRalpha(F318A is likely to account for its apparent "constitutivity." Specific conformational changes suggest the structural basis of pure and partial antagonism. The RAR-RXR heterodimer interface is similar to that observed in most nuclear receptor (NR) homodimers. A correlative analysis of 3D structures and sequences provides a novel view on dimerization among members of the nuclear receptor superfamily.
Authors:
W Bourguet; V Vivat; J M Wurtz; P Chambon; H Gronemeyer; D Moras
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular cell     Volume:  5     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2000 Feb 
Date Detail:
Created Date:  2000-07-17     Completed Date:  2000-07-17     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  289-98     Citation Subset:  IM    
Affiliation:
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CRNS/INSERM/Université Louis Pasteur/Collège de France, Illkirch, Strasbourg.
Data Bank Information
Bank Name/Acc. No.:
PDB/1DKF
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Benzoates / pharmacology
Binding Sites
Crystallography, X-Ray
Dimerization
Fatty Acids / isolation & purification
Humans
Ligands
Mice
Models, Molecular
Molecular Sequence Data
Receptors, Retinoic Acid / antagonists & inhibitors,  chemistry*,  genetics
Recombinant Proteins / chemistry
Retinoid X Receptors
Retinoids / pharmacology
Signal Transduction
Surface Properties
Transcription Factors / chemistry*,  genetics
Chemical
Reg. No./Substance:
0/Benzoates; 0/Fatty Acids; 0/Ligands; 0/Receptors, Retinoic Acid; 0/Recombinant Proteins; 0/Retinoid X Receptors; 0/Retinoids; 0/Transcription Factors; 0/retinoic acid receptor alpha; 146670-40-8/SR 11237

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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