Computer-generated models of blood coagulation factor Xa, factor IXa, and thrombin based upon structural homology with other serine proteases.
Computer-generated molecular models of the trypsin-like domains of blood coagulation factor IXa, Factor Xa, and thrombin have been prepared. These hypothetical models are based upon the sequence homology of the blood coagulation enzymes with the pancreatic serine proteases and the known three-dimensional structure of the pancreatic serine proteases. The internal structures and active sites of these enzymes are highly conserved. The high degree of substrate specificity which characterizes the blood coagulation enzymes appears to be defined not entirely by the active site, but by the unique molecular surface surrounding the active site of each enzyme. Several regions which demonstrate high sequence variability among these enzymes likely participate in forming the putative extended substrate binding sites.
D000595:Amino Acid Sequence; D001779:Blood Coagulation Factors; D003201:Computers; D010450:Endopeptidases; D005164:Factor IX; D015949:Factor IXa; D005170:Factor X; D015951:Factor Xa; D006801:Humans; D008958:Models, Molecular; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship
D001779:Blood Coagulation Factors; D005164:Factor IX; D005170:Factor X; D010450:Endopeptidases; D012697:Serine Endopeptidases; D015949:Factor IXa; D015951:Factor Xa