View source for 5zc1


==X-ray diffraction analysis of the CsStefin-1==
<StructureSection load='5zc1' size='340' side='right'caption='[[5zc1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zc1]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZC1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZC1 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zc1 OCA], [http://pdbe.org/5zc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5zc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zc1 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
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 2.3A. 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 beta-sheets, a central alpha-helix, and a short alpha-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.

Structural basis of the cystein protease inhibitor Clonorchis sinensis Stefin-1.,Park SY, Jeong MS, Park SA, Ha SC, Na BK, Jang SB Biochem Biophys Res Commun. 2018 Mar 25;498(1):9-17. doi:, 10.1016/j.bbrc.2018.02.196. Epub 2018 Feb 28. PMID:29499196<ref>PMID:29499196</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Jang, S B]]
[[Category: Park, S Y]]
[[Category: Cscf]]
[[Category: Csstefin-1]]
[[Category: Cysteine protease inhibitor]]
[[Category: Hydrolase inhibitor]]
[[Category: Immune modulator]]