Recent advances in Cys-loop receptor structure and function.
Throughout the nervous system, moment-to-moment communication relies on postsynaptic receptors to detect neurotransmitters and change the membrane potential. For the Cys-loop superfamily of receptors, recent structural data have catalysed a leap in our understanding of the three steps of chemical-to-electrical transduction: neurotransmitter binding, communication between the binding site and the barrier to ions, and opening and closing of the barrier. The emerging insights might be expected to explain how mutations of receptors cause neurological disease, but the opposite is generally true. Namely, analyses of disease-causing mutations have clarified receptor structure-function relationships as well as mechanisms governing the postsynaptic response.
Department of Physiology, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA. sine@mayo.edu
Steven M
SM
Sine
Andrew G
AG
Engel
D000109:Acetylcholine / Q000378:metabolism; D000818:Animals; D003545:Cysteine; D006801:Humans; D015640:Ion Channel Gating; D020294:Myasthenic Syndromes, Congenital / Q000235:genetics / Q000378:metabolism; D018377:Neurotransmitter Agents / Q000378:metabolism; D018722:Nicotinic Agonists / Q000378:metabolism; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship; D013569:Synapses / Q000502:physiology; D009435:Synaptic Transmission / Q000502:physiology
D018377:Neurotransmitter Agents; D018722:Nicotinic Agonists; D011978:Receptors, Nicotinic; D003545:Cysteine; D000109:Acetylcholine