The intracellular domain of homomeric glycine receptors modulates agonist efficacy
Josip Ivica, Remigijus Lapė, Vid Jazbec, Jie Yu, Hongtao Zhu, Eric Gouaux, Matthew G. Gold, Lucia G. Sivilotti
Abstract
converted taurine and GABA to partial agonists, with maximum open probabilities of 0.66 and 0.40, respectively. Structural comparison of transmembrane helices 3 and 4 in short- and long-ICD GlyR subunits revealed that ICD shortening does not distort the orientation of these helices within each subunit. This suggests that the effects of shortening the ICD stem from removing a modulatory effect of the native ICD on GlyR gating, revealing a new role for the ICD in pentameric ligand-gated channels.
Topics & Concepts
HomomericGlycine receptorTransmembrane domainTaurineGlycineBiophysicsTransmembrane proteinChemistryAgonistProtein subunitIon channelPartial agonistBiochemistryReceptorCell biologyBiologyAmino acidGeneNicotinic Acetylcholine Receptors StudyReceptor Mechanisms and SignalingNeuroscience and Neuropharmacology Research