%0 Journal Article %J The Journal of Steroid Biochemistry and Molecular Biology %D 2010 %T Theoretical study of molecular mechanism of binding TRAP220 coactivator to Retinoid X Receptor alpha, activated by 9-cis retinoic acid %A Mateusz Kurcinski %A Andrzej Koliński %K Binding Sites %K Cell Nucleus %K Cell Nucleus: metabolism %K Computer Simulation %K Crystallography %K Humans %K Ligands %K Mediator Complex Subunit 1 %K Mediator Complex Subunit 1: metabolism %K Models %K Molecular %K Molecular Conformation %K Peptides %K Peptides: chemistry %K Protein Binding %K Protein Structure %K Retinoid X Receptor alpha %K Retinoid X Receptor alpha: metabolism %K Tertiary %K Theoretical %K Tretinoin %K Tretinoin: metabolism %K X-Ray %K X-Ray: methods %X

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.

%B The Journal of Steroid Biochemistry and Molecular Biology %I Elsevier Ltd %V 121 %P 124–9 %8 jul %G eng %U http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2906686&tool=pmcentrez&rendertype=abstract %R 10.1016/j.jsbmb.2010.03.086