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• W2063599549 abstract "Clip-domain serine proteases (SPs) are the essential components of extracellular signaling cascades in various biological processes, especially in embryonic development and the innate immune responses of invertebrates. They consist of a chymotrypsin-like SP domain and one or two clip domains at the N-terminus. Prophenoloxidase-activating factor (PPAF)-II, which belongs to the noncatalytic clip-domain SP family, is indispensable for the generation of the active phenoloxidase leading to melanization, a major defense mechanism of insects. Here, the crystal structure of PPAF-II reveals that the clip domain adopts a novel fold containing a central cleft, which is distinct from the structures of defensins with a similar arrangement of cysteine residues. Ensuing studies demonstrated that PPAF-II forms a homo-oligomer upon cleavage by the upstream protease and that the clip domain of PPAF-II functions as a module for binding phenoloxidase through the central cleft, while the clip domain of a catalytically active easter-type SP plays an essential role in the rapid activation of its protease domain." @default.
• W2063599549 created "2016-06-24" @default.
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• W2063599549 date "2005-12-15" @default.
• W2063599549 modified "2023-10-02" @default.
• W2063599549 title "Crystal structure of a clip-domain serine protease and functional roles of the clip domains" @default.
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• W2063599549 doi "https://doi.org/10.1038/sj.emboj.7600891" @default.
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