Dynamical probing of allosteric control in nuclear receptors.
The dynamical behavior of the nuclear receptor LXR/RXR heterodimer was investigated with molecular dynamics simulations. The simulations reveal correlated motion between residues across the dimer interface that depends significantly on occupation of the ligand binding sites of the monomers. These results are broadly consistent with the observed experimental behavior of the dimers, where structural perturbation is thought to be a key element in signal transduction. Our results provide dynamical support for this model of allosteric control.
Department of Physics and Geology, University of Texas-Pan American , SCIE 3.136 1201 West University Drive, Edinburg, TX 78539-2999, USA. cunningham@utpa.edu
Mark A
MA
Cunningham
D000494:Allosteric Regulation; D008024:Ligands; D000071518:Liver X Receptors; D056004:Molecular Dynamics Simulation; D057093:Orphan Nuclear Receptors / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry*; D047488:Retinoid X Receptors / Q000737:chemistry
D008024:Ligands; D000071518:Liver X Receptors; D057093:Orphan Nuclear Receptors; D018160:Receptors, Cytoplasmic and Nuclear; D047488:Retinoid X Receptors