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The Mode of Action of Soybean Trypsin Inhibitor as Revealed by Crystal Structure Analysis of the Complex with Porcine Trypsin

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Proteinase Inhibitors

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

Abstract

In this paper we would like to accomplish four things:

  1. 1.

    To describe in a general way, and then in some detail, how the soybean trypsin inhibitor (Kunitz) (STI) binds to porcine trypsin, based on X-ray diffraction results to 2.6 Ã… resolution.

  2. 2.

    To show the evidence from which we deduce the structure of the complex at the active site.

  3. 3.

    To explain why this might be a more stable form for the complex than other alternatives.

  4. 4.

    To compare this complex to that of bovine trypsin with the basic pancreatic trypsin inhibitor (Kunitz) [1,2] (PTI).

Supported by Damon Runyon Memorial Fund and the European Molecular Biology Organisation

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References

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© 1974 Springer-Verlag

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Janin, J., Sweet, R.M., Blow, D.M. (1974). The Mode of Action of Soybean Trypsin Inhibitor as Revealed by Crystal Structure Analysis of the Complex with Porcine Trypsin. 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_56

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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_56

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-87968-5

  • Online ISBN: 978-3-642-87966-1

  • eBook Packages: Springer Book Archive

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