1DKF

CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS

Summary for 1DKF

• Entry DOI: 10.2210/pdb1dkf/pdb
• Related: 1LBD 2LBD
• Descriptor: PROTEIN (RETINOID X RECEPTOR-ALPHA), PROTEIN (RETINOIC ACID RECEPTOR-ALPHA), OLEIC ACID, ... (5 entities in total)
• Functional Keywords: helical sandwich, heterodimer, protein-ligand complex, hormone/growth factor receptor, structural proteomics in europe, spine, structural genomics, hormone-growth factor receptor complex
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus: P28700 P10276
• Total number of polymer chains: 2
• Total formula weight: 53301.05

Authors

Bourguet, W.,Vivat, V.,Wurtz, J.M.,Chambon, P.,Gronemeyer, H.,Moras, D.,Structural Proteomics in Europe (SPINE) (deposition date: 1999-12-07, release date: 2000-04-19, Last modification date: 2024-02-07)

Primary citation

Bourguet, W.,Vivat, V.,Wurtz, J.M.,Chambon, P.,Gronemeyer, H.,Moras, D.
Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains.
Mol.Cell, 5:289-298, 2000

PubMed Abstract: 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.

PubMed: 10882070
DOI: 10.1016/S1097-2765(00)80424-4

Experimental method

X-RAY DIFFRACTION (2.5 Å)