ArticleThe Journal of biological chemistry2011
Structure of the M2 transmembrane segment of GLIC, a prokaryotic Cys loop receptor homologue from Gloeobacter violaceus, probed by substituted cysteine accessibility.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 51 citations in OpenAlex.
- Cryo-EM structures of prokaryotic ligand-gated ion channel GLIC provide insights into gating in a lipid environment.Nature communications · 2024Article
- Article
- Chasing the open-state structure of pentameric ligand-gated ion channels.The Journal of general physiology · 2017Article
- Article
- Article
- A Cysteine Substitution Probes β3H267 Interactions with Propofol and Other Potent Anesthetics in α1β3γ2L γ-Aminobutyric Acid Type A Receptors.Anesthesiology · 2016Article
- The Intracellular Loop of the Glycine Receptor: It's not all about the Size.Frontiers in molecular neuroscience · 2016Review
- The atypical cation-conduction and gating properties of ELIC underscore the marked functional versatility of the pentameric ligand-gated ion-channel fold.The Journal of general physiology · 2015Article
- Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.Structure (London, England : 1993) · 2015Article
- Mapping the membrane topography of the TH6-TH7 segment of the diphtheria toxin T-domain channel.The Journal of general physiology · 2015Article
- EPR Studies of Gating Mechanisms in Ion Channels.Methods in enzymology · 2015Review
- Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC).The Journal of biological chemistry · 2014Article
- Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions.PLoS biology · 2013Article
- Cysteine substitutions define etomidate binding and gating linkages in the α-M1 domain of γ-aminobutyric acid type A (GABAA) receptors.The Journal of biological chemistry · 2013Article
- Intermediate closed state for glycine receptor function revealed by cysteine cross-linking.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A gating mechanism of pentameric ligand-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2013Review
- Using molecular dynamics to elucidate the structural basis for function in pLGICs.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Inhibition versus potentiation of ligand-gated ion channels can be altered by a single mutation that moves ligands between intra- and intersubunit sites.Structure (London, England : 1993) · 2013Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
GLIC is a homopentameric proton-gated, prokaryotic homologue of the Cys loop receptor family of neurotransmitter-gated ion channels. Recently, crystal structures of GLIC hypothesized to represent an open channel state were published. To explore the channel structure in functional GLIC channels, we tested the ability of p-chloromercuribenzenesulfonate to react with 30 individual cysteine substitution mutants in and flanking the M2 channel-lining segment in the closed state (pH 7.5) and in a submaximally activated state (pH 5.0). Nine mutants did not tolerate cysteine substitution and were not functional. From positions 10' to 27', p-chloromercuribenzenesulfonate significantly modified the currents at pH 7.5 and 5.0 in all mutants except H234C (11'), I235C (12'), V241C (18'), T243C (20'), L245C (22'), and Y250C (27'), which were not functional, except for 12'. Currents for P246C (23') and K247C (24') were only significantly altered at pH 5.0. The reaction rates were all >1000 m(-1) s(-1). The reactive residues were more accessible in the activated than in the resting state. We infer that M2 is tightly associated with the adjacent transmembrane helices at the intracellular end but is more loosely packed from 10' to the extracellular end than the x-ray structures suggest. We infer that the charge selectivity filter is in the cytoplasmic half of the channel. We also show that below pH 5.0, GLIC desensitizes on a time scale of minutes and infer that the crystal structures may represent a desensitized state.
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