Delineating the Site of Interaction of the 5-HT_3A Receptor with the Chaperone Protein RIC-3.

ABSTRACT: The serotonin type 3A (5-HT_3A) receptor is a homopentameric cation-selective member of the pentameric ligand-gated ion channel (pLGIC) superfamily. Members of this superfamily assemble from five subunits, each of which consists of three domains: extracellular (ECD), transmembrane (TMD), and intracellular domain (ICD). Previously, we have demonstrated that the 5-HT_3A-ICD is required for the interaction between 5-HT_3A and the chaperone protein resistance to inhibitors of choline esterase (RIC-3). Additionally, we have shown that 5-HT_3A-ICD fused to maltose-binding protein (MBP) directly interacts with RIC-3, without the involvement of other protein(s). To elucidate the molecular determinants of this interaction, we developed different MBP-fused 5-H

SUBMITTER: Pirayesh E 

PROVIDER: S-EPMC7036741 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature