10.1371/journal.pone.0107809.g004
John Gatfield
John
Gatfield
Celia Mueller Grandjean
Celia
Mueller Grandjean
Daniel Bur
Daniel
Bur
Martin H. Bolli
Martin H.
Bolli
Oliver Nayler
Oliver
Nayler
Modeling of macitentan (A) and bosentan (B) binding to the active site of the ET<sub>A</sub> receptor.
Public Library of Science
2014
target occupancy
ETA receptor binding pocket
355A
dissociation kinetics
ETA receptor residues
ERA activity
mutation L 322A
ETA receptor dissociation rate
NMR analysis
binding mode
macitentan potencies
acid point mutations
Muscle cells
ETA receptor variants
endothelin binding site
Distinct ETA Receptor Binding Mode
ambrisentan
antagonist activity
bosentan potency
Mutation R 326Q
endothelin receptor antagonists
novel ERA macitentan
ERA interaction site
ETA receptor
2014-09-16 03:04:28
Figure
https://plos.figshare.com/articles/figure/_Modeling_of_macitentan_A_and_bosentan_B_binding_to_the_active_site_of_the_ET_A_receptor_/1171683
<p>The 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 ET<sub>A</sub> 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.</p>