Abstract
Computer-assisted comparisons were made of the X-ray coordinates of all homologous atoms in the serine protease derivatives tosyl chymotrypsin Aα, tosyl elastase, and diisopropylphosphoryl trypsin. The results provided further quantitative support for the belief that sequence homology in proteins results in close similarity of conformation. On this basis, inferences were drawn about the three-dimensional structure of the serine protease thrombin, for which atomic coordinates have not yet been determined experimentally. Further, it was concluded that the unique specificity of thrombin, i.e., its selective cleavage of certain ArgGly bonds in fibrinogen, is unlikely to be due to the insertions in the amino acid sequence of thrombin or to differences in sequence in the region of the active site and binding pocket. It is possible, however, that the elongated A chain appended to thrombin may be a source of this specificity.
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