Pharmacological profiling of sigma 1 receptor ligands by novel receptor homomer assays.

ABSTRACT: The sigma 1 receptor (σ₁R) is a structurally unique transmembrane protein that functions as a molecular chaperone in the endoplasmic reticulum (ER), and has been implicated in cancer, neuropathic pain, and psychostimulant abuse. Despite physiological and pharmacological significance, mechanistic underpinnings of structure-function relationships of σ₁R are poorly understood, and molecular interactions of selective ligands with σ₁R have not been elucidated. The recent crystallographic determination of σ₁R as a homo-trimer provides the foundation for mechanistic elucidation at the molecular level. Here we report novel bioluminescence resonance energy transfer (BRET) assays that enable analyses of ligand-induced multimerization of σ₁R and

SUBMITTER: Yano H 

PROVIDER: S-EPMC5858991 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature