Thermodynamics of the interaction between oxytocin and its myometrial receptor in sheep: a stepwise binding mechanism

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F14%3A43897717" target="_blank" >RIV/60461373:22330/14:43897717 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bcp.2014.06.025" target="_blank" >http://dx.doi.org/10.1016/j.bcp.2014.06.025</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bcp.2014.06.025" target="_blank" >10.1016/j.bcp.2014.06.025</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Thermodynamics of the interaction between oxytocin and its myometrial receptor in sheep: a stepwise binding mechanism

Popis výsledku v původním jazyce

Entropy (deltaS), enthalpy (deltaH) and heat capacity (deltaCp) changes attending the oxytocin interaction with its two binding sites on myometrial cell membranes in sheep were derived from the temperature dependence of Kd values. The high affinity oxytocin site (Kd on the order of 10?9 mol l?1, 25 °C), ascribed to the oxytocin receptor (OXTR), is entropy-driven in the temperature range 0-37 °C. Enthalpy component prevails as a driving force in the binding to the low affinity site (Kd ? 10?7) within thehigher temperature range. deltaCp values in both cases do not differ significantly from zero but become highly relevant in the presence of a GTP analog (10?4 M GTP-gamaS). Under these conditions, deltaCp in the low site interaction becomes negative anddeltaS is shifted toward negative values (enthalpy drift); deltaCp of the high affinity site rises to a high positive value and the interaction is even more strongly entropy driven. Atosiban, a competitive antagonist of oxytocin at OXTR d

Název v anglickém jazyce

Thermodynamics of the interaction between oxytocin and its myometrial receptor in sheep: a stepwise binding mechanism

Popis výsledku anglicky

Entropy (deltaS), enthalpy (deltaH) and heat capacity (deltaCp) changes attending the oxytocin interaction with its two binding sites on myometrial cell membranes in sheep were derived from the temperature dependence of Kd values. The high affinity oxytocin site (Kd on the order of 10?9 mol l?1, 25 °C), ascribed to the oxytocin receptor (OXTR), is entropy-driven in the temperature range 0-37 °C. Enthalpy component prevails as a driving force in the binding to the low affinity site (Kd ? 10?7) within thehigher temperature range. deltaCp values in both cases do not differ significantly from zero but become highly relevant in the presence of a GTP analog (10?4 M GTP-gamaS). Under these conditions, deltaCp in the low site interaction becomes negative anddeltaS is shifted toward negative values (enthalpy drift); deltaCp of the high affinity site rises to a high positive value and the interaction is even more strongly entropy driven. Atosiban, a competitive antagonist of oxytocin at OXTR d

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Biochemical Pharmacology

ISSN

0006-2952

e-ISSN

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Svazek periodika

91

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

119-127

Kód UT WoS článku

000340231300012

EID výsledku v databázi Scopus

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