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Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor Refinement of the Crystal Structure Analysis

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Proteinase Inhibitors

Part of the book series: Bayer-Symposium ((BAYER-SYMP,volume 5))

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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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_55

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-87968-5

  • Online ISBN: 978-3-642-87966-1

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