5ZC1
X-ray diffraction analysis of the CsStefin-1
Summary for 5ZC1
| Entry DOI | 10.2210/pdb5zc1/pdb |
| Descriptor | Cystatin-1 (2 entities in total) |
| Functional Keywords | csstefin-1, cysteine protease inhibitor, immune modulator, cscf, hydrolase inhibitor |
| Biological source | Clonorchis sinensis (Chinese liver fluke) |
| Total number of polymer chains | 6 |
| Total formula weight | 91767.03 |
| Authors | Jang, S.B.,Park, S.Y. (deposition date: 2018-02-14, release date: 2018-12-26, Last modification date: 2024-11-13) |
| Primary citation | 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 Cited by 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: 29499196DOI: 10.1016/j.bbrc.2018.02.196 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.30270802314 Å) |
Structure validation
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