title: Binding energetics of the inhibitor cystatin to the cysteine proteinase actinidin.
abstract: The binding energetics of actinidin to chicken cystatin was determined from fluorometric titrations at different temperatures. It is shown that the association of actinidin with cystatin is both enthalpically and entropically driven, with a negative change in the heat capacity. The molecular basis of these contributions are analyzed within the framework of surface-area models, using a 3D model of the actinidin-cystatin complex, which was obtained using the x-ray structure of the homologous complex papain-stefin B as template.
authors.affiliation: Departamento de Química, Universidad Autónoma Metropolitana Iztapalapa, AP 55-534, México DF, México 09340.
authors.forename: Maricela
authors.initials: M
authors.lastname: Neria-Ríos
authors.forename: Jaqueline
authors.initials: J
authors.lastname: Padilla-Zúñiga
authors.forename: Enrique
authors.initials: E
authors.lastname: Garcia-Hernández
authors.forename: Salvador R
authors.initials: SR
authors.lastname: Tello-Solís
authors.forename: Rafael A
authors.initials: RA
authors.lastname: Zubillaga
mesh_terms: D029042:Actinidia / Q000378:metabolism; D000818:Animals; D002645:Chickens / Q000378:metabolism; D015891:Cystatins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000378:metabolism; D007700:Kinetics
chemical_list: D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases; C018745:actinidain