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


ABSTRACT: IRS-2 from the hard tick Ixodes ricinus belongs to the serpin family of protease inhibitors. It is produced in the salivary glands of the tick and its anti-inflammatory activity suggests that it plays a role in parasite-host interaction. Recombinant IRS-2 prepared by heterologous expression in a bacterial system was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the primitive tetragonal space group P4(3) and diffracted to 1.8?Å resolution. Mass-spectrometric and electrophoretic analyses revealed that IRS-2 was cleaved by contaminating proteases during crystallization. This processing of IRS-2 mimicked the specific cleavage of the serpin by its target protease and resulted in a more stable form (the so-called relaxed 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.

SUBMITTER: Kovarova Z 

PROVIDER: S-EPMC3001646 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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

Kovářová Zuzana Z   Chmelař Jindřich J   Sanda Miloslav M   Brynda Jiří J   Mareš Michael M   Rezáčová Pavlína P  

Acta crystallographica. Section F, Structural biology and crystallization communications 20101028 Pt 11


IRS-2 from the hard tick Ixodes ricinus belongs to the serpin family of protease inhibitors. It is produced in the salivary glands of the tick and its anti-inflammatory activity suggests that it plays a role in parasite-host interaction. Recombinant IRS-2 prepared by heterologous expression in a bacterial system was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the primitive tetragonal space group P4(3) and diffracted to 1.8 Å resolution. Mass-spectrometri  ...[more]

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