Abstract
Structure and Function of the Glycine Receptor and Related Nicotinicoid Receptors
Highlights
Many of the details of GlyR dynamics still remain elusive, the extensive studies conducted on GlyR and other members of the nicotinicoid superfamily in recent years provide us with an emerging picture of the structure and function of these receptors
As novel studies continue to examine these receptors, we are confident that these ion channels will reveal their molecular mechanisms
Acknowledgments—I thank Dr Tommy Tillman for critical reading of this manuscript and Basak Isin for assistance in figure preparation
Summary
The GlyR, as well as all members of the nicotinicoid superfamily of neuroreceptors, has been modeled as having a large extracellular globular domain and four transmembrane (4 TM) ␣-helices per subunit with a large intracellular loop between the third and fourth TM domain (Fig. 1) This “historical” 4 TM helix model was suggested by hydrophobicity plots of the sequences of the ligand-gated channels (8). The periodicity of channel inactivation of systematic Cys mutants provides information regarding local structure This method has been used extensively to examine proposed pore-lining segments in the homologous nAChR (15), serotonin receptor (16, 17), and GABAAR (18). Additional information is needed to more rigorously define a new topological model that reflects the structure of the GlyR and other nicotinicoid receptors
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