Related Experiment Video
Updated: Jul 6, 2026

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
Published on: May 24, 2024
Role of A-chain in functioning of the active site of human alpha-thrombin
M V Kolodzeiskaya1, L I Sokolovskaya, G L Volkov
1Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kiev, Ukraine.
Abstract:
This review summarizes current data suggesting that A-chain of the human alpha-thrombin molecule plays a role of allosteric effector in catalytic reactions with various substrates. Special attention is paid to the relationship between A-chain structure and catalytic activity of thrombin. The existence of this relationship is based on studies of natural mutation of A-chain of the alpha-thrombin molecule. Use of molecular and essential dynamics confirmed the role of A-chain in changes of conformation and catalytic properties of this enzyme; these changes involve residues located in the specificity sites and some inserting loops. Current knowledge on structure and properties of thrombin can be used for the development of new antithrombin agents.
Related Concept Videos
Anticoagulant Drugs: Low-Molecular-Weight Heparins
Extrinsic and Intrinsic Pathways of Hemostasis
The Extrinsic Pathway
The extrinsic pathway of coagulation is typically initiated by tissue damage that exposes blood to tissue factor (TF), a protein released by the damaged tissue cells outside the blood vessels—this interaction with TF triggers biochemical reactions involving specific clotting factors. The key player here is Factor VII, which forms a...
ATP Synthase: Mechanism
Clot Retraction and Fibrinolysis
Chain Reactions
Intracellular Signaling Affects Focal Adhesions
Some...

