Glycine receptor mechanism elucidated by electron cryo-microscopy

• Published in: Nature (London) Vol. 526; no. 7572; pp. 224 - 229
• Main Authors: Du, Juan, Lü, Wei, Wu, Shenping, Cheng, Yifan, Gouaux, Eric
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 08.10.2015; Nature Publishing Group
• Subjects: 101/28; 631/535/1258; 631/92/269; 631/92/612/1237; Allosteric Regulation; Animals; Binding Sites; Biological research; Biology, Experimental; Cryoelectron Microscopy; Glycine - metabolism; Glycine - pharmacology; Glycine receptors; Humanities and Social Sciences; Ion Channel Gating - drug effects; Ivermectin - metabolism; Ivermectin - pharmacology; Ligands; Methods; Microscopy; Models, Molecular; Molecular biology; multidisciplinary; Nervous system; Neurotransmitter Agents - metabolism; Neurotransmitter Agents - pharmacology; Neurotransmitters; Open channels; Pharmacology; Physiological aspects; Protein Conformation - drug effects; Protein Subunits - chemistry; Protein Subunits - drug effects; Protein Subunits - metabolism; Receptors, Glycine - agonists; Receptors, Glycine - antagonists & inhibitors; Receptors, Glycine - metabolism; Receptors, Glycine - ultrastructure; Rotation; Science; Signal Transduction; Strychnine - metabolism; Strychnine - pharmacology; Zebrafish

The strychnine-sensitive glycine receptor (GlyR) mediates inhibitory synaptic transmission in the spinal cord and brainstem and is linked to neurological disorders, including autism and hyperekplexia. Understanding of molecular mechanisms and pharmacology of glycine receptors has been hindered by a...