Conformational transition of the Ixodes ricinus salivary serpin Iripin-4

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F23%3A00572377" target="_blank" >RIV/60077344:_____/23:00572377 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/23:43906526

Výsledek na webu

<a href="https://scripts.iucr.org/cgi-bin/paper?S2059798323002322" target="_blank" >https://scripts.iucr.org/cgi-bin/paper?S2059798323002322</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2059798323002322" target="_blank" >10.1107/S2059798323002322</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Conformational transition of the Ixodes ricinus salivary serpin Iripin-4

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Conformational transition of the Ixodes ricinus salivary serpin Iripin-4

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica Section D-Structural Biology

ISSN

2059-7983

e-ISSN

2059-7983

Svazek periodika

79

Číslo periodika v rámci svazku

MAY

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

409-419

Kód UT WoS článku

000981662200006

EID výsledku v databázi Scopus

2-s2.0-85159555865