title: Allosteric equilibria in the binding of fibrinogen to platelets.
abstract: The binding of fibrinogen to platelets occurs according to the law of mass action. The platelet receptor binds reversibly a single fibrinogen molecule and undergoes a conformational transition between two allosteric states, T and R, that differ in their affinity for fibrinogen. The equilibrium between the two forms is shifted by ADP toward the R (high-affinity) state, thus promoting the aggregation process. This model opens the way to consideration of allosteric modulation of the binding of fibrinogen to its platelet receptor.
authors.affiliation: Istituto di Semeiotica Medica, Universitá Cattolica, Rome, Italy.
authors.forename: R
authors.initials: R
authors.lastname: De Cristofaro
authors.forename: R
authors.initials: R
authors.lastname: Landolfi
authors.forename: E
authors.initials: E
authors.lastname: De Candia
authors.forename: M
authors.initials: M
authors.lastname: Castagnola
authors.forename: E
authors.initials: E
authors.lastname: Di Cera
authors.forename: J
authors.initials: J
authors.lastname: Wyman
mesh_terms: D000244:Adenosine Diphosphate / Q000097:blood / Q000494:pharmacology; D000494:Allosteric Regulation; D001792:Blood Platelets / Q000187:drug effects / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding
chemical_list: D000244:Adenosine Diphosphate; D005340:Fibrinogen