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

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.

SUBMITTER: Kurcinski M

PROVIDER: S-EPMC2906686 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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

Kurcinski Mateusz M Kolinski Andrzej A

The Journal of steroid biochemistry and molecular biology 20100414 1-2

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 ...[more]

PMID: 20398753

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