Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F13%3A43883860" target="_blank" >RIV/60076658:12310/13:43883860 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/12:00381621

Výsledek na webu

<a href="http://link.springer.com/article/10.1007/s00894-012-1505-1" target="_blank" >http://link.springer.com/article/10.1007/s00894-012-1505-1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-012-1505-1" target="_blank" >10.1007/s00894-012-1505-1</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain

Popis výsledku v původním jazyce

The transient receptor potential channel A1 (TRPA1) is unique among ion channels of higher vertebrates in that it harbors a large ankyrin repeat domain. The TRPA1 channel is expressed in the inner ear and in nociceptive neurons. It is involved in hearingas well as in the perception of pungent and irritant chemicals. The ankyrin repeat domain has special mechanical properties, which allows it to function as a soft spring that can be extended over a large range while maintaining structural integrity. A calcium-binding site has been experimentally identified within the ankyrin repeats. We built a model of the N-terminal 17 ankyrin repeat structure, including the calcium-binding EF-hand. In our simulations we find the calcium-bound state to be rigid as compared to the calcium-free state. While the end-to-end distance can change by almost 50% in the apo form, these fluctuations are strongly reduced by calcium binding. This increase in stiffness that constraints the end-to-end distance in t

Název v anglickém jazyce

Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain

Popis výsledku anglicky

The transient receptor potential channel A1 (TRPA1) is unique among ion channels of higher vertebrates in that it harbors a large ankyrin repeat domain. The TRPA1 channel is expressed in the inner ear and in nociceptive neurons. It is involved in hearingas well as in the perception of pungent and irritant chemicals. The ankyrin repeat domain has special mechanical properties, which allows it to function as a soft spring that can be extended over a large range while maintaining structural integrity. A calcium-binding site has been experimentally identified within the ankyrin repeats. We built a model of the N-terminal 17 ankyrin repeat structure, including the calcium-binding EF-hand. In our simulations we find the calcium-bound state to be rigid as compared to the calcium-free state. While the end-to-end distance can change by almost 50% in the apo form, these fluctuations are strongly reduced by calcium binding. This increase in stiffness that constraints the end-to-end distance in t

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EI - Biotechnologie a bionika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

—

Svazek periodika

19

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

4689-4700

Kód UT WoS článku

000326193200009

EID výsledku v databázi Scopus

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