Characterization of the S100A1 Protein Binding Site on TRPC6 C-Terminus
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F13%3A00393088" target="_blank" >RIV/67985823:_____/13:00393088 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1371/journal.pone.0062677" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0062677</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0062677" target="_blank" >10.1371/journal.pone.0062677</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Characterization of the S100A1 Protein Binding Site on TRPC6 C-Terminus
Popis výsledku v původním jazyce
The transient receptor potential (TRP) protein superfamily consists of seven major groups, among them the ?canonical TRP family. The TRPC proteins are calcium-permeable nonselective cation channels activated after the emptying of intracellular calcium stores and appear to be gated by various types of messengers. The TRPC6 channel has been shown to be expressed in various tissues and cells, where it modulates the calcium level in response to external signals. Calcium binding proteins such as Calmodulin or the family of S100A proteins are regulators of TRPC channels. Here we characterized the overlapping integrative binding site for S100A1 at the C-tail of TRPC6, which is also able to accomodate various ligands such as Calmodulin and phosphatidyl-inositol-(4,5)-bisphosphate. Several positively charged amino acid residues (Arg852, Lys856, Lys859, Arg860 and Arg864) were determined by fluorescence anisotropy measurements for their participation in the calcium-dependent binding of S100A1 to
Název v anglickém jazyce
Characterization of the S100A1 Protein Binding Site on TRPC6 C-Terminus
Popis výsledku anglicky
The transient receptor potential (TRP) protein superfamily consists of seven major groups, among them the ?canonical TRP family. The TRPC proteins are calcium-permeable nonselective cation channels activated after the emptying of intracellular calcium stores and appear to be gated by various types of messengers. The TRPC6 channel has been shown to be expressed in various tissues and cells, where it modulates the calcium level in response to external signals. Calcium binding proteins such as Calmodulin or the family of S100A proteins are regulators of TRPC channels. Here we characterized the overlapping integrative binding site for S100A1 at the C-tail of TRPC6, which is also able to accomodate various ligands such as Calmodulin and phosphatidyl-inositol-(4,5)-bisphosphate. Several positively charged amino acid residues (Arg852, Lys856, Lys859, Arg860 and Arg864) were determined by fluorescence anisotropy measurements for their participation in the calcium-dependent binding of S100A1 to
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2013
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
PLoS ONE
ISSN
1932-6203
e-ISSN
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Svazek periodika
8
Číslo periodika v rámci svazku
5
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
6
Strana od-do
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Kód UT WoS článku
000321202100031
EID výsledku v databázi Scopus
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