Structure Comparison of Salivary Serpins from Ixodes ricinus

Barbora Kaščáková¹, Tatyana Prudnikova ¹, Jindřich Chmelař² and Ivana Kutá Smatanová ¹

¹ Institute of Chemistry, Faculty of Science, University of South Bohemia, Branišovská 1760, České Budějovice, Czech Republic

² Department of Medical Biology, Faculty of Science, University of South Bohemia, Branišovská 1760, České Budějovice, Czech Republic

barbora.karaffova@gmail.com

Serine protease inhibitors-serpins is a group of ancient proteins widely distributed in nature (3). Serpins function as serine protease inhibitors but during the evolution, some serpins lost their inhibitory function and serve as molecular chaperones (Heat shock serpin 47), tumor suppressors (Maspin), hormone transporters (Cortisol-binding globulin) or as storage proteins (Ovalbumin) (1). Inhibitory serpins vary in functions according to their specificity and their importance is stressed by serpinopathies, diseases caused by serpin dysfunction or deficiency. Many of today well-known diseases, such as emphysema, cirrhosis, angioedema, hypertension and familial dementia, are associated at least partially by serpin dysfunction (2). This makes serpins interesting candidates for drug development and knowledge of detailed serpin structure is necessary for it.

Fig. 1 Multiple regulatory functions of serpins (From Koiou et al., 2011).

1. Law RH, Zhang Q, McGowan S, et al. An overview of the serpin superfamily. Genome Biol. 2006;7(5):216. doi:10.1186/gb-2006-7-5-216

2. Sanrattana W, Maas C, de Maat S. SERPINs-From Trap to Treatment. Front Med (Lausanne). 2019;6:25. Published 2019 Feb 12. doi:10.3389/fmed.2019.00025

3. Silverman GA, Bird PI, Carrell RW, et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem. 2001;276(36):33293-33296. doi:10.1074/jbc.R100016200