Molecular Mechanisms of Methoctramine Binding and Selectivity at Muscarinic Acetylcholine Receptors

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F14%3A00431597" target="_blank" >RIV/67985823:_____/14:00431597 - isvavai.cz</a>
Alternative codes found
RIV/61389030:_____/14:00431597
Result on the web
<a href="http://dx.doi.org/10.1124/mol.114.093310" target="_blank" >http://dx.doi.org/10.1124/mol.114.093310</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1124/mol.114.093310" target="_blank" >10.1124/mol.114.093310</a>

Result language
angličtina
Original language name
Molecular Mechanisms of Methoctramine Binding and Selectivity at Muscarinic Acetylcholine Receptors
Original language description
We demonstrate that methoctramine high affinity binding to the M2 receptors involves simultaneous interaction with both the orthosteric binding site and the allosteric binding site located between the second and third extracellular loops. Lysine 523 in the third extracellular loop of the M3 receptors forms a hydrogen bond with glutamate 219 of the second extracellular loop that hinders methoctramine binding to the allosteric site at this receptor subtype and results in low affinity of M3 receptor for methoctramine
Czech name
—
Czech description
—

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
ED - Physiology
OECD FORD branch
—

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)