Charybdotoxin Unbinding from the mKv1.3 Potassium Channel: A Combined Computational and Experimental Study
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F11%3A00371168" target="_blank" >RIV/61388955:_____/11:00371168 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/67179843:_____/11:00371168 RIV/60076658:12640/11:43881907
Výsledek na webu
<a href="http://dx.doi.org/10.1021/jp2061909" target="_blank" >http://dx.doi.org/10.1021/jp2061909</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jp2061909" target="_blank" >10.1021/jp2061909</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Charybdotoxin Unbinding from the mKv1.3 Potassium Channel: A Combined Computational and Experimental Study
Popis výsledku v původním jazyce
Charybdotoxin, belonging to the group of so-called scorpiontoxins, is a short peptide able to block many voltage-gated potassium channels, such as mKv1.3, with high affinity. We use a reliable homology model based on the high-resolution crystal structureof the 94% sequence identical homologue Kv1.2 for charybdotoxin docking followed by moleculardynamics simulations to investigate the mechanism and energetics of unbinding, tracing the behavior of the channel protein and charybdotoxin during umbrella-sampling simulations as charybdotoxin is movedaway from the binding site. The potential of mean force is constructed fromthe umbrella sampling simulations and combined with Kd and free energy values gained experimentally using the patch-clamp technique to study the free energy of binding at different ion concentrations andthe mechanism of the charybdotoxin mKv1.3 binding process. A possible charybdotoxin binding mechanism is deduced thatincludes an initial hydrophobic contact followed by st
Název v anglickém jazyce
Charybdotoxin Unbinding from the mKv1.3 Potassium Channel: A Combined Computational and Experimental Study
Popis výsledku anglicky
Charybdotoxin, belonging to the group of so-called scorpiontoxins, is a short peptide able to block many voltage-gated potassium channels, such as mKv1.3, with high affinity. We use a reliable homology model based on the high-resolution crystal structureof the 94% sequence identical homologue Kv1.2 for charybdotoxin docking followed by moleculardynamics simulations to investigate the mechanism and energetics of unbinding, tracing the behavior of the channel protein and charybdotoxin during umbrella-sampling simulations as charybdotoxin is movedaway from the binding site. The potential of mean force is constructed fromthe umbrella sampling simulations and combined with Kd and free energy values gained experimentally using the patch-clamp technique to study the free energy of binding at different ion concentrations andthe mechanism of the charybdotoxin mKv1.3 binding process. A possible charybdotoxin binding mechanism is deduced thatincludes an initial hydrophobic contact followed by st
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EH - Ekologie – společenstva
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2011
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Svazek periodika
115
Číslo periodika v rámci svazku
39
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
11
Strana od-do
11490-11500
Kód UT WoS článku
000295245400021
EID výsledku v databázi Scopus
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