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J Steroid Biochem Mol Biol. 2010 Jul;121(1-2):124-9. doi: 10.1016/j.jsbmb.2010.03.086. Epub 2010 Apr 14.

Theoretical study of molecular mechanism of binding TRAP220 coactivator to Retinoid X Receptor alpha, activated by 9-cis retinoic acid.

Author information

1
Department of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland. mkurc@chem.uw.edu.pl

Abstract

Study on molecular mechanism of conformational reorientation of RXR-alpha ligand binding domain is presented. We employed CABS--a reduced model of protein dynamics to model folding pathways of binding 9-cis retinoic acid to apo-RXR molecule and TRAP220 peptide fragment to the holo form. Based on obtained results we also propose a sequential model of RXR activation by 9-cis retinoic acid and TRAP220 coactivator. Methodology presented here may be used for investigation of binding pathways of other NR/hormone/cofactor sets.

PMID:
20398753
PMCID:
PMC2906686
DOI:
10.1016/j.jsbmb.2010.03.086
[Indexed for MEDLINE]
Free PMC Article

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