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Gating at the Mouth of the Acetylcholine Receptor Channel: Energetic Consequences of Mutations in the αM2-Cap

PLoS One, Jun 2008, Vol.3(6), p.e2515 [Peer Reviewed Journal]

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  • Title:
    Gating at the Mouth of the Acetylcholine Receptor Channel: Energetic Consequences of Mutations in the αM2-Cap
  • Author: Bafna, Pallavi ; Purohit, Prasad ; Auerbach, Anthony
  • Found In: PLoS One, Jun 2008, Vol.3(6), p.e2515 [Peer Reviewed Journal]
  • Subjects: New York ; Physiology ; Receptors ; Amino Acids ; Secondary Structure ; Resistance ; Mutation ; Binding Sites ; Biophysics ; C-Terminus ; Scientific Imaging ; Transmitters ; Energy Measurement ; Proteins ; Mass Spectrometry ; Binding Sites ; Amino Acids ; Conductance ; Residues ; Ligands
  • Language: English
  • Description: Gating of nicotinic acetylcholine receptors from a C(losed) to an O(pen) conformation is the initial event in the postsynaptic signaling cascade at the vertebrate nerve-muscle junction. Studies of receptor structure and function show that many residues in this large, five-subunit membrane protein contribute to the energy difference between C and O. Of special interest are amino acids located at the two transmitter binding sites and in the narrow region of the channel, where C↔O gating motions generate a low↔high change in the affinity for agonists and in the ionic conductance, respectively. We have measured the energy changes and relative timing of gating movements for residues that lie between these two locations, in the C-terminus of the pore-lining M2 helix of the α subunit (‘αM2-cap’). This region contains a binding site for non-competitive inhibitors and a charged ring that influences the conductance of the open pore. αM2-cap mutations have large effects on gating but much smaller...
  • Identifier: E-ISSN: 19326203 ; DOI: 10.1371/journal.pone.0002515

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