Number of the records: 1
Conformational transition of the Ixodes ricinus salivary serpin Iripin-4
- 1.
SYSNO ASEP 0572377 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Conformational transition of the Ixodes ricinus salivary serpin Iripin-4 Author(s) Kascaková, B. (CZ)
Kotál, Jan (BC-A) RID, ORCID
Havlíčková, P. (CZ)
Vopatková, V. (CZ)
Prudnikova, T. (CZ)
Grinkevich, P. (CZ)
Kutý, M. (CZ)
Chmelař, J. (CZ)
Smatanová, I.K. (CZ)Number of authors 9 Source Title Acta Crystallographica Section D-Structural Biology. - : Oxford Blackwell - ISSN 2059-7983
Roč. 79, MAY (2023), s. 409-419Number of pages 7 s. Publication form Online - E Language eng - English Country GB - United Kingdom Keywords serpins ; Iripin-4 ; X-ray structure ; native conformation ; cleaved conformation ; Ixodes ricinus Subject RIV EE - Microbiology, Virology OECD category Microbiology Method of publishing Open access Institutional support BC-A - RVO:60077344 UT WOS 000981662200006 EID SCOPUS 85159555865 DOI 10.1107/S2059798323002322 Annotation Iripin-4, one of the many salivary serpins from Ixodes ricinus ticks with an as-yet unexplained function, crystallized in two different structural conformations, namely the native partially relaxed state and the cleaved serpin. The native structure was solved at a resolution of 2.3 angstrom and the structure of the cleaved conformation was solved at 2.0 angstrom resolution. Furthermore, structural changes were observed when the reactive-centre loop transitioned from the native conformation to the cleaved conformation. In addition to this finding, it was confirmed that Glu341 represents a primary substrate-recognition site for the inhibitory mechanism. The presence of glutamate instead of the typical arginine in the P1 recognition site of all structurally characterized I. ricinus serpins (PDB entries 7b2t, 7pmu and 7ahp), except for the tyrosine in the P1 site of Iripin-2 (formerly IRS-2, PDB entry 3nda), would explain the absence of inhibition of the tested proteases that cleave their substrate after arginine. Further research on Iripin-4 should focus on functional analysis of this interesting serpin. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2024 Electronic address https://scripts.iucr.org/cgi-bin/paper?S2059798323002322
Number of the records: 1