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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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