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Mode of binding of E-64-c, a potent thiol protease inhibitor, to papain as determined by X-ray crystal analysis of the complex. 1989
K Matsumoto, and
D Yamamoto, and
H Ohishi, and
K Tomoo, and
T Ishida, and
M Inoue, and
T Sadatome, and
K Kitamura, and
H Mizuno
Osaka University of Pharmaceutical Sciences, Japan.
The three-dimensional structure of the E-64-c-papain complex has been determined by X-ray crystal analysis at 2.5 A resolution (conventional R = 26.9%). The structure determined indicates that: (i) the C2 atom of the oxirane ring of E-64-c is covalently bound by the S gamma atom of Cys-25 of papain; (ii) this covalent bond formation results in a configurational conversion of the oxirane C2 atom from the S- to the R-form; and (iii) extensive hydrogen bonding and hydrophobic interactions are responsible for the specific interaction of the E-64-c molecule with papain.
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