title: Allostery and coupled sequence variation in nuclear hormone receptors.
abstract: The analysis of correlated sequence variation in evolutionarily related proteins is beginning to provide useful information regarding allosteric coupling between different functional sites. Such an analysis has been carried out for the nuclear hormone receptors, and the conclusions tested by making mutations that switch the allosteric response to ligands of RXR heterodimers.
authors.affiliation: Howard Hughes Medical Institute, Departments of Molecular and Cell Biology and of Chemistry, University of California, Berkeley, CA 94707, USA.
authors.forename: John
authors.initials: J
authors.lastname: Kuriyan
mesh_terms: D000494:Allosteric Regulation / Q000235:genetics; D000595:Amino Acid Sequence / Q000235:genetics; D014644:Genetic Variation / Q000235:genetics; D008024:Ligands; D015233:Models, Statistical; D009154:Mutation / Q000235:genetics; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics* / Q000378:metabolism*
chemical_list: D008024:Ligands; D018160:Receptors, Cytoplasmic and Nuclear