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Báo cáo khoa học: Crystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteases
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A complex of chagasin, a protein inhibitor fromTrypanosoma cruzi, and papain, a classic family C1 cysteine protease, has been crystallized. Kinetic studies revealed that inactivation of papain by chagasin is very fast (kon= 1.5·10 6 m )1 Æs )1 ), and results in the formation of a very tight, reversible complex (Ki =36pm), with similar or better rate and equilib-rium constants than those for cathepsins L and B.
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