期刊
FEBS LETTERS
卷 582, 期 4, 页码 485-490出版社
WILEY
DOI: 10.1016/j.febslet.2008.01.008
关键词
chagasin; cysteine peptidase; inhibitor; mutant; Trypanosoma
资金
- MRC [G9722968] Funding Source: UKRI
- Medical Research Council [G9722968] Funding Source: researchfish
- Medical Research Council [G9722968(65078), G9722968] Funding Source: Medline
- Wellcome Trust [081877] Funding Source: Medline
We have evaluated the roles of key amino acids to the action of the natural inhibitor chagasin of papain-family cysteine peptidases. A W93A substitution decreased inhibitor affinity for human cathepsin L 100-fold, while substitutions of T31 resulted in 10-100-fold increases in the K-i for cruzipain of Trypanosoma cruzi. A T31A/T32A double mutant had increased affinity for cathepsin L but not for cruzipain, while the T31-T32 deletion drastically affected inhibition of both human and parasite peptidases. These differential effects reflect the occurrence of direct interactions between chagasin and helix 8 of cathepsin L, interactions that do not occur with cruzipain. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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