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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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A multipoint hydrogen-bond network underlying KcsA C-type inactivation.

Julio F Cordero-Morales1, Vishwanath Jogini, Sudha Chakrapani

  • 1Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.

Biophysical Journal
|May 18, 2011
PubMed
Summary

A new study reveals a critical hydrogen-bond network involving Trp-67, Glu-71, and Asp-80 in KcsA potassium channel inactivation. This interaction governs selectivity filter dynamics and may be key for other potassium channels.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Structural Biology

Background:

  • Potassium channel gating involves activation at the inner bundle gate and C-type inactivation at the selectivity filter.
  • C-type inactivation in KcsA channels is linked to H-bond interactions between Glu-71 and Asp-80, triggered by inner bundle gate rearrangements.

Purpose of the Study:

  • To investigate the role of the Trp-67 and Asp-80 hydrogen-bond interaction in KcsA C-type inactivation.
  • To explore the analogous role of similar residue interactions in Kv channels.

Main Methods:

  • Investigated hydrogen-bond pairings between specific residues in KcsA potassium channels.
  • Examined equivalent interactions in Shaker and Kv1.2 channels to assess conserved roles.

Main Results:

  • Identified a critical H-bond interaction between Trp-67 and Asp-80 that dictates the rate and extent of KcsA C-type inactivation.
  • Disruption of analogous interactions in Shaker and Kv1.2 channels modulated their inactivation processes.
  • Demonstrated that KcsA C-type inactivation is governed by a multipoint hydrogen-bond network (Trp-67-Glu71-Asp-80).

Conclusions:

  • The Trp-67-Glu71-Asp-80 triad is crucial for the dynamics and conformational stability of the KcsA selectivity filter.
  • This triad may act as a general modulator for selectivity filter gating across the potassium channel family.