Glycine receptor

Glycine receptor‏‎

The Glycine receptor (GlyR) is a member of a family of ligand-gated ion channels that mediate fast synaptic inhibition in the central nervous system. This receptor is predominantly expressed in the spinal cord and brainstem, where it plays a crucial role in the transmission of inhibitory post-synaptic potentials.

Structure

The Glycine receptor is a pentameric protein composed of five subunits. Each subunit is formed by four transmembrane domains (TM1-TM4) and a large extracellular N-terminal domain. The receptor's pentameric structure forms a central pore that is permeable to chloride ions when the receptor is activated by glycine.

Function

The primary function of the Glycine receptor is to mediate inhibitory neurotransmission. When glycine binds to the receptor, it causes a conformational change that opens the chloride ion channel. This allows chloride ions to flow into the neuron, which hyperpolarizes the cell membrane and inhibits the generation of action potentials.

Clinical significance

Mutations in the genes encoding the Glycine receptor subunits can lead to a range of neurological disorders, including hyperekplexia, a condition characterized by an exaggerated startle response. In addition, GlyR dysfunction has been implicated in the pathogenesis of certain types of epilepsy and chronic pain.

Pharmacology

Several drugs are known to interact with the Glycine receptor, including strychnine, which is a potent antagonist, and alcohol, which is a positive allosteric modulator. These interactions can modulate the receptor's function and have potential therapeutic applications.

See also

• Neurotransmitter receptor
• GABA receptor
• Neurotransmission

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  Glycine_receptor

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  Glycine receptor structure with agonists and antagonists