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Resting state of the human proton channel dimer in a lipid bilayer

Li, Qufei ; Shen, Rong ; Treger, Jeremy S. ; Wanderling, Sherry S. ; Milewski, Wieslawa ; Siwowska, Klaudia ; Bezanilla, Francisco ; Perozo, Eduardo

Proceedings of the National Academy of Sciences - PNAS, 2015-11, Vol.112 (44), p.E5926-E5935 [Periódico revisado por pares]

United States: National Academy of Sciences

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  • Título:
    Resting state of the human proton channel dimer in a lipid bilayer
  • Autor: Li, Qufei ; Shen, Rong ; Treger, Jeremy S. ; Wanderling, Sherry S. ; Milewski, Wieslawa ; Siwowska, Klaudia ; Bezanilla, Francisco ; Perozo, Eduardo
  • Assuntos: Amino Acid Sequence ; Biological Sciences ; Dimerization ; Humans ; Ion Channel Gating ; Ion Channels - chemistry ; Ion Channels - metabolism ; Lipid Bilayers ; Lipids ; Membranes ; Molecular Sequence Data ; PNAS Plus ; Protons ; Spectrum analysis
  • É parte de: Proceedings of the National Academy of Sciences - PNAS, 2015-11, Vol.112 (44), p.E5926-E5935
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
    Author contributions: Q.L. and E.P. designed research; Q.L., R.S., J.S.T., S.S.W., W.M., and K.S. performed research; F.B. contributed new reagents/analytic tools; Q.L., R.S., and J.S.T. analyzed data; and Q.L. and E.P. wrote the paper.
    Edited by David E. Clapham, Howard Hughes Medical Institute, Boston Children's Hospital, Boston, MA, and approved September 10, 2015 (received for review July 29, 2015)
  • Descrição: The voltage-gated proton channel Hv1 plays a critical role in the fast proton translocation that underlies a wide range of physiological functions, including the phagocytic respiratory burst, sperm motility, apoptosis, and metastatic cancer. Both voltage activation and proton conduction are carried out by a voltage-sensing domain (VSD) with strong similarity to canonical VSDs in voltage-dependent cation channels and enzymes. We set out to determine the structural properties of membrane-reconstituted human proton channel (hHv1) in its resting conformation using electron paramagnetic resonance spectroscopy together with biochemical and computational methods. We evaluated existing structural templates and generated a spectroscopically constrained model of the hHv1 dimer based on the Ci-VSD structure at resting state. Mapped accessibility data revealed deep water penetration through hHv1, suggesting a highly focused electric field, comprising two turns of helix along the fourth transmembrane segment. This region likely contains the H⁺ selectivity filter and the conduction pore. Our 3D model offers plausible explanations for existing electrophysiological and biochemical data, offering an explicit mechanism for voltage activation based on a one-click sliding helix conformational rearrangement.
  • Editor: United States: National Academy of Sciences
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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