Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick Ixodes ricinus

0349395 - ÚOCHB 2011 RIV GB eng J - Journal Article
Kovářová, Zuzana - Chmelař, Jindřich - Šanda, Miloslav - Brynda, Jiří - Mareš, Michael - Řezáčová, Pavlína
Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick Ixodes ricinus.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. F66, č. 11 (2010), s. 1453-1457. ISSN 1744-3091. E-ISSN 2053-230X
R&D Projects: GA ČR(CZ) GAP207/10/2183; GA MŠMT(CZ) LC06009
Institutional research plan: CEZ:AV0Z40550506; CEZ:AV0Z60220518; CEZ:AV0Z50520514
Keywords : protease inhibitor * serpin * tick * proteolysis
Subject RIV: CE - Biochemistry
Impact factor: 0.563, year: 2010

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.
Permanent Link: http://hdl.handle.net/11104/0189648