title: The structural basis of allosteric regulation in proteins.
abstract: Allosteric regulation of protein function occurs when the regulatory trigger, such as the binding of a small-molecule effector or inhibitor, takes place some distance from the protein's, or protein complex's, active site. This distance can be a few A, or tens of A. Many proteins are regulated in this way and exhibit a variety of allosteric mechanisms. Here we review how analyses of experimentally determined models of protein 3D structures, using either X-ray crystallography or NMR spectroscopy, have revealed some of the mechanisms involved.
authors.affiliation: European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, United Kingdom. roman@ebi.ac.uk
authors.forename: Roman A
authors.initials: RA
authors.lastname: Laskowski
authors.forename: Fabian
authors.initials: F
authors.lastname: Gerick
authors.forename: Janet M
authors.initials: JM
authors.lastname: Thornton
mesh_terms: D000494:Allosteric Regulation; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011506:Proteins