Allosteric Equilibria in the Binding of Fibrinogen to Platelets

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 betwe...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-11, Vol.85 (22), p.8473-8476
Main Authors: De Cristofaro, Raimondo, Landolfi, Raffaele, De Candia, Erica, Castagnola, Massimo, Di Cera, Enrico, Wyman, Jeffries
Format: Article
Language:English
Subjects:
Adenosine Diphosphate - blood
Adenosine Diphosphate - pharmacology
Allosteric Regulation
Binding sites
Biochemistry
Biological and medical sciences
Biophysics
Blood coagulation. Blood cells
Blood Platelets - drug effects
Blood Platelets - metabolism
Coagulation factors
fibrinogen
Fibrinogen - metabolism
Fundamental and applied biological sciences. Psychology
Humans
Kinetics
Logarithms
man
Mathematical constants
Molecular and cellular biology
Molecules
Parametric models
Platelets
Protein Binding
Radioactive decay
Receptors
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.22.8473