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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pavlova A,Krupa JC,Mort JS,Abrahamson M,Björk Idoi
10.1016/s0014-5793(00)02337-1keywords:
subject
Has Abstractpub_date
2000-12-29 00:00:00pages
156-60issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02337-1journal_volume
487pub_type
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