| First Author | Bourguet W | Year | 2000 |
| Journal | Mol Cell | Volume | 5 |
| Issue | 2 | Pages | 289-98 |
| PubMed ID | 10882070 | Mgi Jnum | J:320125 |
| Mgi Id | MGI:6869964 | Doi | 10.1016/s1097-2765(00)80424-4 |
| Citation | Bourguet W, et al. (2000) Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell 5(2):289-98 |
| abstractText | 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. |
