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Aspartate 112 is the selectivity filter of the human voltage-gated proton channel

Author

Listed:
  • Boris Musset

    (Rush University Medical Center)

  • Susan M. E. Smith

    (Emory School of Medicine)

  • Sindhu Rajan

    (University of Chicago)

  • Deri Morgan

    (Rush University Medical Center)

  • Vladimir V. Cherny

    (Rush University Medical Center)

  • Thomas E. DeCoursey

    (Rush University Medical Center)

Abstract

Aspartate key to proton selectivity Voltage-gated proton channels are considered completely selective for protons — no evidence exists for the permeation of ions other than H+. A study of the underlying mechanism of the high selectivity of the human voltage-gated proton channel reveals an Asp112 residue as the selectivity filter. When this residue was changed to a neutral amino acid, the mutant channel lost proton selectivity and either became anion-selective or did not conduct any ions.

Suggested Citation

  • Boris Musset & Susan M. E. Smith & Sindhu Rajan & Deri Morgan & Vladimir V. Cherny & Thomas E. DeCoursey, 2011. "Aspartate 112 is the selectivity filter of the human voltage-gated proton channel," Nature, Nature, vol. 480(7376), pages 273-277, December.
    • Handle: RePEc:nat:nature:v:480:y:2011:i:7376:d:10.1038_nature10557
    DOI: 10.1038/nature10557
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    Cited by:

    1. Spencer C. Guo & Rong Shen & Benoît Roux & Aaron R. Dinner, 2024. "Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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