Abstract
The serine proteinases and their natural inhibitors interact very strongly and specifically. There is evidence that enzymatic catalysis is involved in this interaction [1, 2]. The structure analysis of the free pancreatic trypsin inhibitor (PTI) has suggested that it is ideally shaped to cover the active site area of the serine proteinases [3, 4], This was borne out by model building studies with α-chymo-trypsin and PTI [5] and by the crystal structure analysis of the complex of trypsin with PTI [6].
Supported by the Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 51 and the Royal Society European Fellowship (A. J.).
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Huber, R., Kukla, D., Steigemann, W., Deisenhofer, J., Jones, A. (1974). Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor Refinement of the Crystal Structure Analysis. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_55
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