GLRA1 Membrane Protein Introduction

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
Gene Name GLRA1
Aliases Glycine receptor 48 kDa subunit, Glycine receptor strychnine-binding subunit
Organism Homo sapiens (Human)
UniProt ID P23415
Transmembrane Times 4
Length (aa) 457

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.

Structure of ligand-gated ion channels.Fig.1 Structure of ligand-gated ion channels. (Haverkamp, 2012)

Application of GLRA1 Membrane Protein in Literature

  1. Safar F., et al. The Startle Disease Mutation E103K Impairs Activation of Human Homomeric α1 Glycine Receptors by Disrupting an Intersubunit Salt Bridge across the Agonist Binding Site. J Biol Chem. 2017, 292(12): 5031-5042. PubMed ID: 28174298

    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.

  2. Welsh B.T., et al. Disruption of a putative intersubunit electrostatic bond enhances agonist efficacy at the human α1 glycine receptor. Brain Res. 2017, 1657: 148-155. PubMed ID: 27923639

    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.

  3. Zhang Y., et al. Investigating the Mechanism by Which Gain-of-function Mutations to the α1 Glycine Receptor Cause Hyperekplexia. J Biol Chem. 2016, 291(29): 15332-41. PubMed ID: 27226610

    The article indicates that perlecan binds the clustering molecule gliomedin and enhances clustering of a node of Ranvier components.

  4. Moraga-Cid G., et al. Allosteric and hyperekplexic mutant phenotypes investigated on an α1 glycine receptor transmembrane structure. Proc Natl Acad Sci U S A. 2015, 112(9): 2865-70. PubMed ID: 25730860

    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.

  5. Burgos C.F., et al. Evidence for α-helices in the large intracellular domain mediating modulation of the α1-glycine receptor by ethanol and Gβγ. J Pharmacol Exp Ther. 2015, 352(1): 148-55. PubMed ID: 25339760

    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

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-GLRA1 antibody development services.

As a leading service provider, Creative Biolabs is proud to present our professional service in membrane protein preparation and help you with the research of membrane proteins. Please do not hesitate to inquire us for more details.


  1. Haverkamp S, et al. (2012). Glycine Receptor Diversity in the Mammalian Retina. The Organization of the Retina and Visual System.

All listed customized services & products are for research use only, not intended for pharmaceutical, diagnostic, therapeutic or any in vivo human use.

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