Molecular determinants involved in differential behaviour between soluble tissue factor and full-length tissue factor towards factor VIIa
Author:
Affiliation:
1. Department of Biological Chemistry
2. Indian Association for the Cultivation of Science
3. Kolkata
4. India
Abstract
During blood-coagulation, the transmembrane protein tissue factor (TF) binds to its ligand, factor (F)VII, activating and allosterically modifying it to form a mature active binary complex (TF–FVIIa).
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP02179H
Reference40 articles.
1. Biochemistry and Physiology of Blood Coagulation
2. An ordered addition, essential activation model of the tissue factor pathway of coagulation: evidence for a conformational cage
3. High Affinity Ca2+-binding Site in the Serine Protease Domain of Human Factor VIIa and Its Role in Tissue Factor Binding and Development of Catalytic Activity
4. Cooperative Interaction of Divalent Metal Ions, Substrate, and Tissue Factor with Factor VIIa
5. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
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4. In Silico Mutation and Binding Studies of Human FVIIa γ-Carboxyglutamic Acid-Domain to Endothelial Protein C Receptor: A Molecular Dynamics Simulation Approach;ACS Omega;2019-01-08
5. Contribution of allosteric disulfide in the structural regulation of membrane-bound tissue factor–factor VIIa binary complex;Journal of Biomolecular Structure and Dynamics;2018-11-13
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