All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Resonance assignment of coiled-coil 3 (CC3) domain of human STIM1

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43904250" target="_blank" >RIV/60076658:12310/21:43904250 - isvavai.cz</a>

  • Result on the web

    <a href="https://link.springer.com/article/10.1007/s12104-021-10042-7" target="_blank" >https://link.springer.com/article/10.1007/s12104-021-10042-7</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s12104-021-10042-7" target="_blank" >10.1007/s12104-021-10042-7</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Resonance assignment of coiled-coil 3 (CC3) domain of human STIM1

  • Original language description

    The protein stromal interaction molecule 1 (STIM1) plays a pivotal role in mediating store-operated calcium entry (SOCE) into cells, which is essential for adaptive immunity. It acts as a calcium sensor in the endoplasmic reticulum (ER) and extends into the cytosol, where it changes from an inactive (tight) to an active (extended) oligomeric form upon calcium store depletion. NMR studies of this protein are challenging due to its membrane-spanning and aggregation properties. Therefore follow the divide-and-conquer approach, focusing on individual domains first is in order. The cytosolic part is predicted to have a large content of coiled-coil (CC) structure. We report the H-1, C-13, N-15 chemical shift assignments of the CC3 domain. This domain is crucial for the stabilisation of the tight quiescent form of STIM1 as well as for activating the ORAI calcium channel by direct contact, in the extended active form.

  • 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

    10610 - Biophysics

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biomolecular NMR Assignments

  • ISSN

    1874-2718

  • e-ISSN

  • Volume of the periodical

    15

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    433-439

  • UT code for WoS article

    000687015200001

  • EID of the result in the Scopus database

    2-s2.0-85113167452