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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

Biomolecular NMR Assignments

ISSN

1874-2718

e-ISSN

—

Svazek periodika

15

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

433-439

Kód UT WoS článku

000687015200001

EID výsledku v databázi Scopus

2-s2.0-85113167452