期刊
BIOCHEMISTRY
卷 57, 期 3, 页码 267-276出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.7b00891
关键词
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资金
- National Institutes of Health (NIH) [F31 NS093838]
- NIH [R01 NS083660, R01 CA206573]
- Amgen Young Investigator Award
- Irma T. Hirschl Career Scientist Award
Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that mediate the majority of excitatory rieurotransniission in the central nervous system, iGluRs open their ion channels in response to binding of the neurotransmitter glutamate, rapidly depolarize the postsynaptic neuronal membrane, and initiate signal transduction. Recent Studies using X-ray crystallography and cryo-electron microscopy have determined full-length iGluR structures that (1) uncover the receptor architecture in an unliganded, resting state, (2) reveal conformational changes produced by ligands in order to activate iGluRs, open their ion channels, and conduct ions; and (8) Show how activated, glutamate-bound iGluRs can adopt a nonconducting desensitized state. These new findings, combined with the results of previous structural and functional experiments, kinetic and, molecular modeling, mutagenesis, and biochemical analyses; provide :new views on the structural mechanisms of iGluR gating.
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