5ZC1

X-ray diffraction analysis of the CsStefin-1

5ZC1 の概要

• エントリーDOI: 10.2210/pdb5zc1/pdb
• 分子名称: Cystatin-1 (2 entities in total)
• 機能のキーワード: csstefin-1, cysteine protease inhibitor, immune modulator, cscf, hydrolase inhibitor
• 由来する生物種: Clonorchis sinensis (Chinese liver fluke)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 91767.03

構造登録者

Jang, S.B.,Park, S.Y. (登録日: 2018-02-14, 公開日: 2018-12-26, 最終更新日: 2024-11-13)

主引用文献

Park, S.Y.,Jeong, M.S.,Park, S.A.,Ha, S.C.,Na, B.K.,Jang, S.B.
Structural basis of the cystein protease inhibitor Clonorchis sinensis Stefin-1.
Biochem. Biophys. Res. Commun., 498:9-17, 2018

PubMed Abstract: Cystein protease plays a critical role as a virulence factor in the development and progression of various diseases. Cystatin is a superfamily of cysteine protease inhibitors that participates in various physiological and pathological processes. The cysteine protease inhibitor CsStein-1 isolated from Clonorchis sinensis belongs to the type 1 stefin of cystatins. This inhibitor regulates the activity and processing of CsCF (Cathepsin F of Clonorchis sienesis), which plays an important role in parasite nutrition and host-parasite interaction. CsStefin-1 has also been proposed as a host immune modulator and a participant in the mechanism associated with anti-inflammatory ability. Here, we report the first crystal structure of CsStefin-1 determined by the multi-wavelength anomalous diffraction (MAD) method to 2.3 Å. There are six molecules of CsStefin-1 per asymmetric unit, with a solvent content of 36.5%. The structure of CsStefin-1 is composed of twisted four-stranded antiparallel β-sheets, a central α-helix, and a short α-helix. We also demonstrate that CsStefin-1 binds to CsCF-8 cysteine protease and inhibits its activity. In addition, a molecular docking model of CsStefin-1 and CsCF-8 was developed using homology modeling based on their structures. The structural information regarding CsStefin-1 and molecular insight into its interaction with CsCF-8 are important to understanding their biological function and to design of inhibitors that modulate cysteine protease activity.

PubMed: 29499196
DOI: 10.1016/j.bbrc.2018.02.196

実験手法

X-RAY DIFFRACTION (2.30270802314 Å)