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The aimof this workwas to elucidate the roles of individualresidues within the flexible second binding loop of humancystatin A in the inhibition of cysteine proteases. Fourrecombinant variants of the inhibitor, each with a singlemutation, L73G, P74G, Q76G or N77G, in the mostexposed part of this loopwere generated by PCR-based site-directed mutagenesis. The binding of these variants topapain, cathepsin L, and cathepsin B was characterized byequilibrium and kinetic methods.
Nội dung trích xuất từ tài liệu:
Báo cáo Y học: The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73
