Structure of a serpin–protease complex shows inhibition by deformation

By J. Huntington, Randy J. Read, R. Carrell. Nature, 2000

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How researchers see this paper

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Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases (2010, background): “The distortion of the catalytic site structure prevents the release of the protease from the complex, and the structural disorder induces its proteolytic inactivation (Huntington et al., 2000).”
Plant protease inhibitors: a defense strategy in plants (2007, background): “The cleavage of an appropriate peptide bond in the reactive centre loop of the inhibitor triggers a rapid conformational change so that catalysis does not proceed beyond the formation of an acyl-enzyme complex (Huntington et al., 2000).”
An overview of the serpin superfamily (2006, background): “These structural studies [12,35,36], combined”
Consensus protein design (2016, background): “Inhibitory members fold to a metastable native state that undergoes a major conformational change in order to inhibit target proteases (Huntington et al., 2000).”