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

Agrim Gupta; Manuel Kitzler; Petr Rathner; Marc Fahrner; Herwig Grabmayr; Adriana Rathner; Christoph Romanin; Norbert Müller

doi:10.1007/s12104-021-10042-7

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

Agrim Gupta, Manuel Kitzler, Petr Rathner, Marc Fahrner, Herwig Grabmayr, Adriana Rathner, Christoph Romanin, Norbert Müller

Research output: Contribution to journal › Article › peer-review

Abstract

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 1H, 13C, 15N 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.

Original language	English
Pages (from-to)	433-439
Number of pages	7
Journal	Biomolecular NMR Assignments
Volume	15
Issue number	2
DOIs	https://doi.org/10.1007/s12104-021-10042-7
Publication status	Published - 2021

Fields of science

104 Chemistry
104021 Structural chemistry
104026 Spectroscopy
104015 Organic chemistry
104017 Physical chemistry
106002 Biochemistry
106041 Structural biology
301305 Medical chemistry
302043 Magnetic resonance imaging (MRI)

JKU Focus areas

Sustainable Development: Responsible Technologies and Management

Access to Document

10.1007/s12104-021-10042-7

Cite this

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title = "Resonance assignment of coiled-coil 3 (CC3) domain of human STIM1",

abstract = "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 1H, 13C, 15N 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.",

author = "Agrim Gupta and Manuel Kitzler and Petr Rathner and Marc Fahrner and Herwig Grabmayr and Adriana Rathner and Christoph Romanin and Norbert M{\"u}ller",

year = "2021",

doi = "10.1007/s12104-021-10042-7",

language = "English",

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journal = "Biomolecular NMR Assignments",

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T1 - Resonance assignment of coiled-coil 3 (CC3) domain of human STIM1

AU - Gupta, Agrim

AU - Kitzler, Manuel

AU - Rathner, Petr

AU - Fahrner, Marc

AU - Grabmayr, Herwig

AU - Rathner, Adriana

AU - Romanin, Christoph

AU - Müller, Norbert

PY - 2021

Y1 - 2021

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AB - 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 1H, 13C, 15N 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.

U2 - 10.1007/s12104-021-10042-7

DO - 10.1007/s12104-021-10042-7

M3 - Article

SN - 1874-2718

VL - 15

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JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

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