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The role of conserved residues of chagasin in the inhibition of cysteine peptidases.

dos Reis, Flavia C G; Smith, Brian O; Santos, Camila C; Costa, Tatiana F R; Scharfstein, Julio; Coombs, Graham H; Mottram, Jeremy C; Lima, Ana Paula C A.
FEBS Lett; 582(4): 485-90, 2008 Feb 20.
Artigo em Inglês | MEDLINE | ID: mdl-18201565
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.
Selo DaSilva