@article {Kurcinski2010, title = {Theoretical study of molecular mechanism of binding TRAP220 coactivator to Retinoid X Receptor alpha, activated by 9-cis retinoic acid}, journal = {The Journal of Steroid Biochemistry and Molecular Biology}, volume = {121}, number = {1-2}, year = {2010}, month = {jul}, pages = {124{\textendash}9}, publisher = {Elsevier Ltd}, abstract = {

Study on molecular mechanism of conformational reorientation of RXR-alpha ligand binding domain is presented. We employed CABS{\textendash}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.

}, keywords = {Binding Sites, Cell Nucleus, Cell Nucleus: metabolism, Computer Simulation, Crystallography, Humans, Ligands, Mediator Complex Subunit 1, Mediator Complex Subunit 1: metabolism, Models, Molecular, Molecular Conformation, Peptides, Peptides: chemistry, Protein Binding, Protein Structure, Retinoid X Receptor alpha, Retinoid X Receptor alpha: metabolism, Tertiary, Theoretical, Tretinoin, Tretinoin: metabolism, X-Ray, X-Ray: methods}, issn = {1879-1220}, doi = {10.1016/j.jsbmb.2010.03.086}, url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2906686\&tool=pmcentrez\&rendertype=abstract}, author = {Mateusz Kurcinski and Andrzej Koli{\'n}ski} }