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• W2034175085 startingPage "203" @default.
• W2034175085 abstract "Proregions of papain-like cysteine proteases are potent and often highly selective inhibitors of their parental enzymes. The molecular basis of their selectivity is poorly understood. For two closely related members of the cathepsin L-like subfamily we established strong selectivity differences. The propeptide of cathepsin S was observed to inhibit cathepsin L with a K(i) of 0.08 nM, yet cathepsin L propeptide inhibited cathepsin S only poorly. To identify the respective structural correlates we engineered chimeric propeptides and compared their inhibitory specificity with the wild-types. Specificity resided in the N-terminal part, strongly suggesting that the backbone of the prodomain was the underlying structure." @default.
• W2034175085 created "2016-06-24" @default.
• W2034175085 creator A5004439886 @default.
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• W2034175085 date "2000-03-08" @default.
• W2034175085 modified "2023-09-30" @default.
• W2034175085 title "The α1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L‐like cysteine protease subfamily" @default.
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• W2034175085 doi "https://doi.org/10.1016/s0014-5793(00)01281-3" @default.
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