title: Switching cation-binding loops paves the way for redesigning allosteric activation.
authors.affiliation: Chemistry Department, University of Louisville, Louisville, KY 40292, USA. muriel.maurer@louisville.edu
authors.forename: Muriel C
authors.initials: MC
authors.lastname: Maurer
mesh_terms: D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002412:Cations / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011486:Protein C / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D013917:Thrombin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D002412:Cations; D011486:Protein C; D013917:Thrombin