Abstract
In this paper we would like to accomplish four things:
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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.
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2.
To show the evidence from which we deduce the structure of the complex at the active site.
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3.
To explain why this might be a more stable form for the complex than other alternatives.
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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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Private communication from R. HUBER.
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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
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