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
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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
10610 - Biophysics
Result continuities
Project
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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
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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