Abstract
THE protein trypsin inhibitors are proteins which bind very strongly to trypsin, blocking its active site (Ki = 10−9 to 10−14 M) we have carried out a crystal structure analysis of the complex of soybean trypsin inhibitor (Kunitz) (STI), one of the largest inhibitors, with porcine trypsin. Huber and his colleagues have determined the structure of a complex of a small inhibitor, bovine pancreatic trypsin inhibitor (Kunitz) (PTI), with bovine trypsin1. These studies improve our understanding of the catalytic mechanism of trypsin, demonstrate that various trypsin inhibitors act in a similar way and provide insight into the development of strong, specific binding between protein molecules.
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BLOW, D., JANIN, J. & SWEET, R. Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein–protein interactions. Nature 249, 54–57 (1974). https://doi.org/10.1038/249054a0
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DOI: https://doi.org/10.1038/249054a0
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