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1dkf

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(New page: 200px<br /> <applet load="1dkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkf, resolution 2.50&Aring;" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:26, 12 November 2007

Image:1dkf.gif

1dkf, resolution 2.50Å

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

Contents

Overview

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.

Disease

Known disease associated with this structure: Leukemia, acute promyelocytic OMIM:[180240]

About this Structure

1DKF is a Protein complex structure of sequences from Homo sapiens and Mus musculus with BMS and OLA as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains., Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D, Mol Cell. 2000 Feb;5(2):289-98. PMID:10882070

Page seeded by OCA on Mon Nov 12 16:33:23 2007

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