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- W2080800689 abstract "The crystal structure of a catalytically inactive form of cathepsin D (CatD hi ) has been obtained at pH 7.5. The N-terminal strand relocates by 30 Å from its position in the interdomain β-sheet and inserts into the active site cleft, effectively blocking substrate access. CatD hi has a five-stranded interdomain β-sheet and resembles Intermediate 3 , a hypothetical structure proposed to be transiently formed during proteolytic activation of the proenzyme precursor. Interconversion between active and inactive forms of CatD is reversible and may be regulated by an ionizable switch involving the carboxylate side chains of Glu 5, Glu 180, and Asp 187. Our findings provide a structural basis for the pH-dependent regulation of aspartic proteinase activity and suggest a novel mechanism for pH-dependent modulation of substrate specificity." @default.
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- W2080800689 date "1998-10-01" @default.
- W2080800689 modified "2023-09-26" @default.
- W2080800689 title "Conformational switching in an aspartic proteinase" @default.
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- W2080800689 doi "https://doi.org/10.1038/2306" @default.
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