Biopolym. Cell. 1994; 10(6):83-87.
http://dx.doi.org/10.7124/bc.0003C8
Modelling of thrombin-fibrinogen recognition complex
1Karabut L. V., 1Shchechkin I. E., 1Serejskaya A. A.
  1. Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine
    1, Murmans'ka Str., Kyiv, Ukraine, 02094

Abstract

Fibrinogen-thrombin recognition complex consisting of enzyme additional binding exosite (ABE) and complementary site (CS) ir fibrinogen Aa-chain has been investigated by means of molecular modelling and conformational computer simulations. It is revealed that four hydrogen bonds between ABE and CS occur the distance between donor and acceptor atoms being 2.0–2.2 A. Energy estimations show that these interactions can ensure creation of energetically reliable complex of the thrombin with fibrinogen beyond the enzyme active center. Hypothesis is proposed that conformational changes arising in consequence of recognition complex formation may lead to promotion of catalytical process.
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