TY - JOUR T1 - Theoretical study of molecular mechanism of binding TRAP220 coactivator to Retinoid X Receptor alpha, activated by 9-cis retinoic acid JF - The Journal of Steroid Biochemistry and Molecular Biology Y1 - 2010 A1 - Mateusz Kurcinski A1 - Andrzej Koliński KW - Binding Sites KW - Cell Nucleus KW - Cell Nucleus: metabolism KW - Computer Simulation KW - Crystallography KW - Humans KW - Ligands KW - Mediator Complex Subunit 1 KW - Mediator Complex Subunit 1: metabolism KW - Models KW - Molecular KW - Molecular Conformation KW - Peptides KW - Peptides: chemistry KW - Protein Binding KW - Protein Structure KW - Retinoid X Receptor alpha KW - Retinoid X Receptor alpha: metabolism KW - Tertiary KW - Theoretical KW - Tretinoin KW - Tretinoin: metabolism KW - X-Ray KW - X-Ray: methods AB -

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.

PB - Elsevier Ltd VL - 121 UR - http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2906686&tool=pmcentrez&rendertype=abstract ER -