Biochemistry (Moscow)

, 73:237 | Cite as

Role of A-chain in functioning of the active site of human α-thrombin

  • M. V. Kolodzeiskaya
  • L. I. SokolovskayaEmail author
  • G. L. Volkov


This review summarizes current data suggesting that A-chain of the human α-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 α-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.

Key words

thrombin allosterics mutagenesis protein C modulation thrombomodulin molecular dynamics 



basic pancreatic thrombin inhibitor


essential dynamics


molecular dynamics




protease-activated receptor 1




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Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  • M. V. Kolodzeiskaya
    • 1
  • L. I. Sokolovskaya
    • 1
    Email author
  • G. L. Volkov
    • 1
  1. 1.Palladin Institute of BiochemistryNational Academy of Sciences of UkraineKievUkraine

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