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Glycine receptor (GlyR)-mediated inhibitory neurotransmitter in the mammalian central nervous system (CNS) reflex activity, regulation of voluntary movement and sensory signal processing plays an important role in [1]. GlyR pentamer of three independent peptides: the two-glycoprotein (48 kD and 58 kD), are known as α and β subunit, and the other for the 93 kD cytoplasmic protein, called "gephyrin". GlyR and the nicotine acetylcholine receptor (nAChR), GABAA receptor (GABAAR) ,5-HT3 receptor (5-HT3R) and other great homology. Together they form a ligand-gated ion channels (LGICs) superfamily. Five LGICs the formation of transmembrane ion channel subunit foramen. On GlyR, the ion channel selective permeability Cl-. A, GlyR distribution in the CNS glyR in the spinal cord and medulla oblongata in a high level of expression, and in the midbrain, hypothalamus and thalamus in the lower brain areas are not high-level expression. This distribution pattern of GlyR and Gly in the spinal cord and brain stem as the major inhibitory neurotransmitter in line to play a role. It is interesting to note, GlyR and GABAAR often co-exist in the spinal cord neurons [2], suggesting that Gly and GABA transmitters may be used as a total (cotransmitter), in the spinal cord play a total transfer (cotransmission) role [3,4]. From the adult rat spinal cord GlyR purified by the α1 and β subunits of the different polymer components, roughly in the ratio of α1： β = 3:2. In contrast, there is evidence that the embryos of five GlyR is composed of α2 subunit with the dimer. Α2 in vitro with the reorganization of polymer and the functional characteristics of embryonic GlyR is also very consistent. In addition, the spinal cord in rats found only low levels of α3 mRNA, prompted α3 may be accounted for in the proportion of GlyR smaller. β subunit is not easy to form a separate polymer with GlyR, but effectively with α1， α2 or α3 different polymer combination. On the other hand, even in the absence of β subunit， α1， α2 and α3 form a reorganization can also GlyR. α1 subunit mRNA distribution and adult spinal cord and brain stem in the 3H-strychnine binding site is similar to. However, it was surprising that the β subunit to the high number of mRNA in the adult CNS in a whole. The existence of high-level brain regions β subunit mRNA and some people difficult to understand, because the β subunit can not form a separate function of GlyR. GlyR subunit intracellular gephyrin more extensive distribution of mRNA in the rat CNS expression in all regions. Although GlyR in adult animals, almost lack of higher brain areas such as, but in the acute separation and primary culture of neonatal rat hippocampal neurons have been observed by the Gly-induced current response. Recently, Flint, etc. [5] reported that during the early development of rat neocortex, non-synaptic release of taurine can activate GlyR area. Embryonic period as a result of taurine can lead to deprivation of cortical dysplasia. That taurine may therefore activate non-synaptic GlyR affected parts of the development of neocortex. In the sub-cellular level, GlyR to "cluster" approach in the cell surface. It is assumed in the cell body and dendrites of the "cluster" is located on the synaptic connections. In the process of cell culture, gephyrin to the GlyR cluster is necessary, gephyrin can be anchored receptor on the cell cytoskeleton. In addition, recent studies have shown that early in embryonic development, the activation of excitatory GlyR not have inhibitory effects [6,7], GlyR a "cluster" is due to glycine receptor activation caused by voltage-dependent Ca2 + channel openers, and the resulting influx of Ca2 + regulation [7]. Second, GlyR molecular structure (A) the structure of GlyRα subunit and β subunit each from the 420 and 470 amino acid residues (figure). By hydrophobicity analysis, forecasts GlyR subunit with a long extracellular N-terminal area, four transmembrane domain (referred to as M1-M4) and a home between the M3-M4 loop of the large cells. This is the general model structure LGICs. N-terminal of the GlyR contains at least one potential N-glycosylation sites (such as α1 first 38 residues N), this area is likely to exist two pairs of sulfur chain. Central is the first Cys-138 and Cys-152 （α1 subunit counting）, through disulfide bond formation, the ring is at all conservative LGICs; M1 second ring around the district, is Cys-198 and the formation of Cys-209. In the α and β subunit M3 and M4 cells between the inner ring large initial Department, there are some positively charged residues and contains protein kinase phosphorylation sequence. (B) receptor assembly a。