ArticleBiochemistry2002
Structure of the transition state of gating in the acetylcholine receptor channel pore: a phi-value analysis.
Article in Biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Mechanism of hydrophobic gating in the acetylcholine receptor channel pore.The Journal of general physiology · 2024Article
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- Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe.Accounts of chemical research · 2021Review
- Chasing the open-state structure of pentameric ligand-gated ion channels.The Journal of general physiology · 2017Article
- 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
- Article
- 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
- Hydrophobic interactions between the voltage sensor and pore mediate inactivation in Kv11.1 channels.The Journal of general physiology · 2013Article
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Pore helices play a dynamic role as integrators of domain motion during Kv11.1 channel inactivation gating.The Journal of biological chemistry · 2013Article
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- Conformational transitions underlying pore opening and desensitization in membrane-embedded Gloeobacter violaceus ligand-gated ion channel (GLIC).The Journal of biological chemistry · 2012Article
- End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.Physiological reviews · 2012Review
- The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel.The Journal of general physiology · 2012Article
- Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Effects of lipid-analog detergent solubilization on the functionality and lipidic cubic phase mobility of the Torpedo californica nicotinic acetylcholine receptor.The Journal of membrane biology · 2011Article
- Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating.The Journal of general physiology · 2011Article
- Mapping heat exchange in an allosteric protein.Biophysical journal · 2011Article
- Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel.Nature structural & molecular biology · 2011Article
- Subunit symmetry at the extracellular domain-transmembrane domain interface in acetylcholine receptor channel gating.The Journal of biological chemistry · 2010Article
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3 authors.
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Abstract
The gating mechanism of the acetylcholine receptor channel (AChR) was investigated by using rate equilibrium linear free energy relationships (LFERs) to probe the transition state between the closed and open conformations. The properties of the transition state of gating in the second transmembrane segment (M2) of the delta subunit, one of the five homologous pore-lining segments, was measured on a residue-by-residue basis. Series of point mutations were engineered at individual positions of this domain, and the corresponding constructs were characterized electrophysiologically, at the single-channel level. Fully liganded AChR opening and closing rate constants were estimated, and Phi-values (which are a measure of the extent of the conformational change realized at the transition state) were calculated for each reaction series as the slope of the Brønsted relationship (log rate constant versus log equilibrium constant). Our results indicate that, at the transition state of gating, the extracellular half of deltaM2 partly resembles the open state (Phi-values between 0.24 and 0.38) while the intracellular half completely resembles the closed state (Phi-values between -0.18 and 0.03), with a break point near the middle of the M2 segment. This suggests that during gating the two halves of deltaM2 move asynchronously, with the rearrangement of the extracellular portion preceding (following) that of the intracellular part of deltaM2 during opening (closing). This particular sequence of molecular events indicates that the gating conformational change, which starts at the extracellular acetylcholine-binding sites (when opening), does not propagate exclusively along the primary sequence of the protein. In addition, our data are consistent with the deltaM2 segment bending or swiveling around its central residues during gating. We also elaborate on unsettled aspects of the analysis such as the accuracy of two-point LFERs, the physical interpretation of fractional Phi-values, and the existence of single versus parallel transition states for the gating reaction.
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