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      Serine protease inhibitors in plants: nature’s arsenal crafted for insect predators

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          Most cited references219

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          Protease Inhibitors in Plants: Genes for Improving Defenses Against Insects and Pathogens

          C Ryan (1990)
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            Structure of a serpin-protease complex shows inhibition by deformation.

            The serpins have evolved to be the predominant family of serine-protease inhibitors in man. Their unique mechanism of inhibition involves a profound change in conformation, although the nature and significance of this change has been controversial. Here we report the crystallographic structure of a typical serpin-protease complex and show the mechanism of inhibition. The conformational change is initiated by reaction of the active serine of the protease with the reactive centre of the serpin. This cleaves the reactive centre, which then moves 71 A to the opposite pole of the serpin, taking the tethered protease with it. The tight linkage of the two molecules and resulting overlap of their structures does not affect the hyperstable serpin, but causes a surprising 37% loss of structure in the protease. This is induced by the plucking of the serine from its active site, together with breakage of interactions formed during zymogen activation. The disruption of the catalytic site prevents the release of the protease from the complex, and the structural disorder allows its proteolytic destruction. It is this ability of the conformational mechanism to crush as well as inhibit proteases that provides the serpins with their selective advantage.
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              Evolutionary families of peptidase inhibitors.

              The proteins that inhibit peptidases are of great importance in medicine and biotechnology, but there has never been a comprehensive system of classification for them. Some of the terminology currently in use is potentially confusing. In the hope of facilitating the exchange, storage and retrieval of information about this important group of proteins, we now describe a system wherein the inhibitor units of the peptidase inhibitors are assigned to 48 families on the basis of similarities detectable at the level of amino acid sequence. Then, on the basis of three-dimensional structures, 31 of the families are assigned to 26 clans. A simple system of nomenclature is introduced for reference to each clan, family and inhibitor. We briefly discuss the specificities and mechanisms of the interactions of the inhibitors in the various families with their target enzymes. The system of families and clans of inhibitors described has been implemented in the MEROPS peptidase database (http://merops.sanger.ac.uk/), and this will provide a mechanism for updating it as new information becomes available.
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                Author and article information

                Journal
                Phytochemistry Reviews
                Phytochem Rev
                Springer Science and Business Media LLC
                1568-7767
                1572-980X
                March 2013
                May 4 2012
                March 2013
                : 12
                : 1
                : 1-34
                Article
                10.1007/s11101-012-9231-y
                d31bb86e-c82c-448e-8e08-9e90798409a3
                © 2013

                http://www.springer.com/tdm

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