Crystal structure of human cathepsin S.
作者： Mary E Mcgrath , James T Palmer , Ddeter Brömme , John R Somoza , None
关键词: Cysteine 、 Cathepsin S 、 Papain 、 Binding site 、 Scissile bond 、 Cysteine protease 、 Enzyme binding 、 Chemistry 、 Crystallography 、 Stereochemistry 、 Cathepsin
摘要: We have determined the 2.5 A structure (Rcryst = 20.5%, Rfree 28.5%) of a complex between human cathepsin S and potent, irreversible inhibitor 4-morpholinecarbonyl-Phe-hPhe-vinyl sulfone-phenyl. Noncrystallographic symmetry averaging other density modification techniques were used to improve electron maps which nonoptimal due systematically incomplete data. Methods that reduce number parameters implemented for refinement. The refined shows be similar related cysteine proteases such as papain cathepsins K L. As expected, covalently-bound is attached enzyme at Cys 25, binding subsites S3-S1' are occupied by respective substituents. somewhat larger S2 pocket than what found in enzymes consistent with broader specificity this site, while Lys 61 S3 site may offer opportunities selective inhibition enzyme. presence Arg 137 S1' pocket, proximal 25 implications not only substrate C-terminal scissile bond, but also catalysis.
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