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Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick Ixodes ricinus
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SYSNO ASEP 0349395 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick Ixodes ricinus Author(s) Kovářová, Zuzana (UOCHB-X) RID, ORCID
Chmelař, Jindřich (BC-A)
Šanda, Miloslav (UOCHB-X)
Brynda, Jiří (UMG-J) RID
Mareš, Michael (UOCHB-X) RID, ORCID
Řezáčová, Pavlína (UOCHB-X) RID, ORCIDNumber of authors 6 Source Title Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
F66, č. 11 (2010), s. 1453-1457Number of pages 5 s. Language eng - English Country GB - United Kingdom Keywords protease inhibitor ; serpin ; tick ; proteolysis Subject RIV CE - Biochemistry R&D Projects GAP207/10/2183 GA ČR - Czech Science Foundation (CSF) LC06009 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40550506 - UOCHB-X (2005-2011) AV0Z60220518 - PAU-O, BC-A (2005-2011) AV0Z50520514 - UMG-J (2005-2011) UT WOS 000283714100011 DOI 10.1107/S1744309110032343 Annotation IRS-2 from the hard tick Ixodes ricinus belongs into the serpin family of protease inhibitors. It is produced in the tick salivary glands, and its anti-inflammatory activity suggests a role in the parasitehost interaction. Recombinant IRS-2 prepared by heterologous expression in bacterial system was crystallized and crystals diffracted to resolution 1.8 Å. IRS-2 was cleaved during crystallization by contaminating proteases. This processing of IRS-2 mimicked the specific cleavage of serpin by its target protease and resulted in a more stable R conformation, which produced well-diffracting crystals. Activity profiling with specific substrates and inhibitors demonstrated traces of serine and cysteine proteases in the protein stock solution. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2011
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