Fig. 5.  Monod–Wyman–Changeux two-state equilibrium model for etomidate and GABA activation of GABAAreceptors. The scheme depicts allosteric coagonism for GABAAreceptors with two equivalent GABA (G ; orthosteric agonist) sites and two equivalent etomidate (E ; allosteric agonist) sites. The L0parameter describes the basal equilibrium between the two canonical states: inactive (R ) and active (O ). KGis the dissociation constant for GABA interactions with R -state receptors; and KG* is the dissociation constant for GABA interactions with O -state receptors. The GABA efficacy factor, c , is defined as KG*/KG. KEis the dissociation constant for etomidate interactions with R -state receptors; and K  E* is the dissociation constant for etomidate interactions with O -state receptors. The etomidate efficacy factor, d , is defined as KE*/KE. The differently sized arrows  illustrate how equilibria shift as ligands bind and functional state changes.

Fig. 5.  Monod–Wyman–Changeux two-state equilibrium model for etomidate and GABA activation of GABAAreceptors. The scheme depicts allosteric coagonism for GABAAreceptors with two equivalent GABA (G ; orthosteric agonist) sites and two equivalent etomidate (E ; allosteric agonist) sites. The L0parameter describes the basal equilibrium between the two canonical states: inactive (R ) and active (O ). KGis the dissociation constant for GABA interactions with R -state receptors; and KG* is the dissociation constant for GABA interactions with O -state receptors. The GABA efficacy factor, c , is defined as KG*/KG. KEis the dissociation constant for etomidate interactions with R -state receptors; and K  E* is the dissociation constant for etomidate interactions with O -state receptors. The etomidate efficacy factor, d , is defined as KE*/KE. The differently sized arrows  illustrate how equilibria shift as ligands bind and functional state changes.

Close Modal

or Create an Account

Close Modal
Close Modal