ALLOSTERIC REGULATION OF THE BLOOD CLOTTING CASCADE

Abstract

Recognition of functional partners is a pivotal factor in the regulation of protein interactions. The areas of direct contact between complementary molecules that interact according to Koshland’s "key - lock" scheme deserve special attention. The relevance of the study of this kind of interactions is obvious. In the case of the simplest serine proteinases the increased affinity of the enzyme to a certain area of the target protein is ensured by the synchronous interaction of the binding and allosteric sub-sites with amino acid residues of the target protein, that are adequate by ligand specificity and placed in an optimal conformation. The purpose of this work is to clarify the compliance of the components of the blood clotting cascade with this rule. Comparison of the primary sequences of sites of activation cleavage, reactive centers of serpins and sites of proteolytic inactivation testifies in favor of this assumption.