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• W2022205354 endingPage "160" @default.
• W2022205354 startingPage "156" @default.
• W2022205354 abstract "Cystatins A and C were both shown to inhibit cathepsin B by a two-step mechanism, involving an initial weak interaction followed by a conformational change. Disruption of the major salt bridge anchoring the occluding loop of cathepsin B to the main body of the enzyme by mutation of His110 to Ala converted the binding to an apparent one-step reaction. The second step of cystatin binding to cathepsin B must therefore be due to the inhibitor having to alter the conformation of the enzyme by displacing the occluding loop to allow a tight complex to be formed. Cystatin A was appreciably less effective in displacing the loop than cystatin C, resulting in a considerably lower overall inhibition rate constant." @default.
• W2022205354 created "2016-06-24" @default.
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• W2022205354 date "2000-12-29" @default.
• W2022205354 modified "2023-09-26" @default.
• W2022205354 title "Cystatin inhibition of cathepsin B requires dislocation of the proteinase occluding loop. Demonstration by release of loop anchoring through mutation of His110" @default.
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• W2022205354 doi "https://doi.org/10.1016/s0014-5793(00)02337-1" @default.
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