[HTML][HTML] Modeling and mutagenesis of the binding site of Calhex 231, a novel negative allosteric modulator of the extracellular Ca2+-sensing receptor
C Petrel, A Kessler, F Maslah, P Dauban… - Journal of Biological …, 2003 - ASBMB
A model of the Ca 2+-sensing receptor (CaSR) seven transmembrane domains was
constructed based on the crystal structure of bovine rhodopsin. This model was used for
docking (1S, 2S, 1′ R)-N 1-(4-chlorobenzoyl)-N 2-[1-(1-naphthyl) ethyl]-1, 2-
diaminocyclohexane (Calhex 231), a novel potent negative allosteric modulator that blocks
(IC 50= 0.39 μm) increases in [3 H] inositol phosphates elicited by activating the human wild-
type CaSR transiently expressed in HEK293 cells. In this model, Glu-837 7.39 plays a …
constructed based on the crystal structure of bovine rhodopsin. This model was used for
docking (1S, 2S, 1′ R)-N 1-(4-chlorobenzoyl)-N 2-[1-(1-naphthyl) ethyl]-1, 2-
diaminocyclohexane (Calhex 231), a novel potent negative allosteric modulator that blocks
(IC 50= 0.39 μm) increases in [3 H] inositol phosphates elicited by activating the human wild-
type CaSR transiently expressed in HEK293 cells. In this model, Glu-837 7.39 plays a …
