Mode of binding of E‐64‐c, a potent thiol protease inhibitor, to papain as determined by X‐ray crystal analysis of the complex

FEBS Letters

Matsumoto, Keita²  Tomoo, Kouji²  Ohishi, Hirofumi²  Inoue, Masatoshi²  Sadatome, Takahisa¹  Ishida, Toshimasa²  Kitamura, Kunihiro¹  Mizuno, Hiroshi³  Yamamoto, Daisuke² 

[1] Research Center, Taisho Pharmaceutical Co. Ltd, 1-403 Yoshino-cho, Ohmiya, Saitama 330 Japan;Osaka University of Pharmaceutical Sciences, 2-10-65 Kawai, Matsubara, Osaka 580 Japan;Department of Molecular Biology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki 305, Japan

关键词: E-64-c;    Papain;    Enzyme-inhibitor complex;    X-ray crystal analysis;   

DOI  :  10.1016/0014-5793(89)80216-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The three-dimensional structure of the E-64-c-papain complex has been determined by X-ray crystal analysis at 2.5 Å 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^γ 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.

【 授权许可】

Unknown