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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 1999/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papain-CLIK148 complex |
| 執筆形態 | その他 |
| 掲載誌名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
| 出版社・発行元 | ACADEMIC PRESS INC |
| 巻・号・頁 | 266(2),pp.411-416 |
| 担当区分 | 筆頭著者,最終著者 |
| 著者・共著者 | H Tsuge,T Nishimura,Y Tada,T Asao,D Turk,Turk, V,N Katunuma |
| 概要 | Papain was used as an experimental model structure to understand the inhibition mechanism of newly developed specific inhibitors of cathepsin L, the papain superfamily. Recently, we developed a series of cathepsin L-specific inhibitors which are called the CLIK series [(1999) FEBS Lett. 458, 6-10]. Here, we report the complex structure of papain with CLIK148, which is a representative inhibitor from the CLIK series. The inhibitor complex structure was solved at 1.7 ii resolution with conventional R 0.177. Unlike other epoxisuccinate inhibitors (E64, CA030, and CA074), CLIK148 uses both prime and nonprime sites, which are important for the specific inhibitory effect on cathepsin L. Also, the specificity for cathepsin L could be explained by the existence of Phe in the P2 site and hydrophobic interaction of N-terminal pyridine ring. (C) 1999 Academic Press. |
| DOI | 10.1006/bbrc.1999.1830 |
| ISSN | 0006-291X |