Figure_4.tif (6.77 MB)
Modeling of macitentan (A) and bosentan (B) binding to the active site of the ETA receptor.
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posted on 2014-09-16, 03:04 authored by John Gatfield, Celia Mueller Grandjean, Daniel Bur, Martin H. Bolli, Oliver NaylerThe amino acid residues predicted to contact macitentan and/or bosentan are grouped into the categories “nearest neighbors”, “ERA charge interaction” and “extended ERA binding pocket”. (C) Conformations of macitentan (red) and bosentan (green) bound to ETA as proposed by molecular modeling. Relevant structural differences are (1) the different head groups, (2) the length of the central rigid axis spanning over the head group and either one (macitentan) or two (bosentan) pyrimidines, (3) the presence or absence of the 5-bromo-pyrimidine stacking onto the core pyrimidine.
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target occupancyETA receptor binding pocket355Adissociation kineticsETA receptor residuesERA activitymutation L 322AETA receptor dissociation rateNMR analysisbinding modemacitentan potenciesacid point mutationsMuscle cellsETA receptor variantsendothelin binding siteDistinct ETA Receptor Binding Modeambrisentanantagonist activitybosentan potencyMutation R 326Qendothelin receptor antagonistsnovel ERA macitentanERA interaction siteETA receptor
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