Influence of the N Terminus on the Biophysical Properties and Pharmacology of TREK1 Potassium Channels
Molecular Pharmacology Elsevier 85:5 (2014) 671-681
Structural and Thermodynamic Characterization of the Gating Pathway in a K+ Channel
BIOPHYSICAL JOURNAL 106:2 (2014) 155A-155A
Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.
J Biol Chem 289:1 (2014) 143-151
Abstract:
KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating.A Novel Mechanism of Voltage Sensing and Gating in K2P Potassium Channels
Biophysical Journal Elsevier 106:2 (2014) 746a
A novel mechanism of voltage sensing and gating in K2P potassium channels
ACTA PHYSIOLOGICA 210 (2014) 62-62