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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Bourguet W,Vivat V,Wurtz JM,Chambon P,Gronemeyer H,Moras Ddoi
10.1016/s1097-2765(00)80424-4subject
Has Abstractpub_date
2000-02-01 00:00:00pages
289-98issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80424-4journal_volume
5pub_type
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