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Communication between N terminus and loop2 tunes Orai activation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F18%3A00489833" target="_blank" >RIV/61388971:_____/18:00489833 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.saa.2017.12.021" target="_blank" >http://dx.doi.org/10.1016/j.saa.2017.12.021</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.saa.2017.12.021" target="_blank" >10.1016/j.saa.2017.12.021</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Communication between N terminus and loop2 tunes Orai activation

  • Original language description

    The CRAC channel gating involves the binding of STIM1 C-terminus to cytosolic N- and C-termini of Orai. The C-termini of Orai is the main binding partner however N-termini also have been found necessary for Orai channel function. Despite a highly conserved ETON region Orai1 and Orai3 differ in length of the ETON region. Our aim here was to study the reasons for different behavior of these two isoforms and to find the differences in structural requirement for gating and function. While there is no interaction between the N-terminus and loop2 in Orai3, we predict that interactions between loop2 and Orai1 N-terminus results into masking the STIM1 coupling sites which are located either at N-terminus or loop2 or both, thus loop2 either directly or allosterically affects the STIM1-Orai coupling in an isoform specific manner. Thus along with the requirement of conserved ETON region a fine tuning between N-termini and loop2 conformations has an essential role in maintaining permissive conformation of channel and store-operated function of Orai channel.nn

  • 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

    <a href="/en/project/LTC17069" target="_blank" >LTC17069: Understanding different aspects of structure and function of cation translocation systems.</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    293

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

    1271-1285

  • UT code for WoS article

    000423515000014

  • EID of the result in the Scopus database

    2-s2.0-85041209005