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Structural insights into serpin—protease complexes reveal the inhibitory mechanism of serpins

Nature Structural Biology volume 4, pages 354–357 (1997)Cite this article

Analysis of native serpin–protease complexes indicate that inhibition by serpins involves reactive centre cleavage and partial loop insertion, whereby the covalently linked protease migrates from the position of the initial attack to a position on the surface of the inhibitor β-sheet A to form a virtually irreversible complex.

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Authors and Affiliations

  1. Departments of Medical Biochemistry and Biophysics, Umeå University, S-901 87, Umeå, Sweden

    Malgorzata Wilczynska, Ming Fa, Per-Ingvar Ohlsson & Tor Ny

  2. Physical Chemistry, Umeå University, S-901 87, Umeå, Sweden

    Jan Karolin & Lennart B-Å. Johansson

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  1. Malgorzata Wilczynska
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  2. Ming Fa
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Wilczynska, M., Fa, M., Karolin, J. et al. Structural insights into serpin—protease complexes reveal the inhibitory mechanism of serpins. Nat Struct Mol Biol 4, 354–357 (1997). https://doi.org/10.1038/nsb0597-354

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