Conformational transition of the Ixodes ricinus salivary serpin Iripin-4
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60076658:12310/23:43906526
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Conformational transition of the Ixodes ricinus salivary serpin Iripin-4
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section D-Structural Biology
ISSN
2059-7983
e-ISSN
2059-7983
Volume of the periodical
79
Issue of the periodical within the volume
MAY
Country of publishing house
GB - UNITED KINGDOM
Number of pages
7
Pages from-to
409-419
UT code for WoS article
000981662200006
EID of the result in the Scopus database
2-s2.0-85159555865