Introduction of GLRA1
Glycine receptor subunit alpha-1 (GLRA1), also known as Glycine receptor 48 kDa subunit or Glycine receptor strychnine-binding subunit, is a protein that in humans is encoded by the GLRA1 gene. Glycine receptors (GlyR) are members of the cys-loop family of ligand-gated ion channels, responsible for mediating the inhibitory effects of glycine. They are widely distributed throughout the CNS, particularly within the hippocampus, spinal cord, and brain stem. Most GlyR in adults is composed of α1β heteromers, but α1 subunits can also form functional homomeric receptors in many expression systems. Glycine is thought to be the endogenous ligand for synaptic GlyR, but evidence exists that taurine tonically activates extrasynaptic GlyR.
|Basic Information of GLRA1|
|Protein Name||Glycine receptor subunit alpha-1|
|Aliases||Glycine receptor 48 kDa subunit, Glycine receptor strychnine-binding subunit|
|Organism||Homo sapiens (Human)|
Function of GLRA1 Membrane Protein
Glycine receptors (GlyR) belong to the pentameric ligand-gated ion channel (pLGIC) superfamily and mediate fast inhibitory transmission in the vertebrate CNS. The disruption of glycinergic transmission through inherited mutations can cause panic disease in humans. Many startle mutations that are in GlyRs provide useful clues to the function of the channel domains. Glycine receptor subunit alpha-1 protein mediates postsynaptic inhibition in the CNS. Defects in the GLRA1 gene are a cause of startle disease, also known as congenital stiff-person syndrome or hereditary hyperekplexia. Multiple transcript variants encoding different isoforms have been found. Diseases associated with GLRA1 include Hyperekplexia, Hereditary 1 and Hyperekplexia. Among its related pathways are peptide ligand-binding receptors and DAG and IP3 signaling.
Fig.1 Structure of ligand-gated ion channels. (Haverkamp, 2012)
Application of GLRA1 Membrane Protein in Literature
The study reveals that the startle disease mutation E103K impairs the activation of the human homomeric α1 glycine receptors by disrupting an intersubunit salt bridge across the agonist binding site.
The article reports that the determination of the efficacy following ligand binding to the glycine receptor may involve the disruption of an intersubunit electrostatic interaction occurring near the agonist binding site.
The article indicates that perlecan binds the clustering molecule gliomedin and enhances clustering of a node of Ranvier components.
Authors in this group investigate the allosteric and hyperekplexic mutant phenotypes on an α1 glycine receptor transmembrane structure. The first X-ray structure of the TMD of the α1GlyR using GLIC as a scaffold paves the way for mechanistic studies and the design of allosteric modulators of human receptors.
This article reports that α-helices in the large intracellular domain mediate modulation of the α1-glycine receptor by ethanol and Gβγ.
GLRA1 Preparation Options
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