Structural Features of the Proteins Participating in Blood Coagulation and Fibrinolysis

In recent years, a great deal of new information has emerged regarding the structure and function of the various proteins involved in blood coagulation, fibrinolysis, complement activation, and other physiological events that occur in blood. The structural data for these proteins have been obtained by a combination of amino acid sequence analysis of purified preparations and cDNA cloning. This information has made it clear that there are many common structures or domains that are shared by the plasma proteins and other proteins from different tissues and organs. For example, the carboxy-terminal 250–300 amino acids that constitute the catalytic domain in the serine proteases of plasma show a high degree of amino acid sequence homology with pancreatic trypsin (Katayama et al. 1979). The function of this domain in the plasma serine proteases is to catalyze the hydrolysis of arginine-containing peptide bonds. It contains the triad of serine, histidine, and aspartic acid...