The adult form of the GlyR is the heteromeric α1β receptor, which is believed to have a stoichiometry (proportion) of three α1 subunits and two β subunits
 or four α1 subunits and one β subunit. The α-subunits are also able to form functional homo-pentameric receptors in heterologous expression systems in African clawed frog'soocytes or mammalian cell lines, and the α1 homomeric receptor is essential for studies of channel pharmacokinetics and pharmacodynamics.
Auxiliary β subunit is unable to form functional channels without association with α subunits. However, previous reports have demonstrated that β subunit determines the synaptic localization of GlyRs, as well as the pharmacological profile of glycinergic currents
Glycine receptors in diseases
Disruption of GlyR surface expression or reduced ability of expressed GlyRs to conduct chloride ions results in the rare neurological disorder, hyperekplexia. The disorder is characterized by an exaggerated response to unexpected stimuli which is followed by a temporary but complete muscular rigidity often resulting in an unprotected fall. Chronic injuries as a result of the falls are symptomatic of the disorder. A mutation in GLRA1 is responsible for some cases of stiff person syndrome.
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