Journal
BIOPHYSICAL JOURNAL
Volume 99, Issue 9, Pages L72-L74Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2010.08.069
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Funding
- GENCI-CINES [2009-075137]
- National Institutes for Health [GM 40712]
- National Council of Technological and Scientific Development [471590/2009-6]
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The effects on the structural and functional properties of the Kv1.2 voltage-gated ion channel, caused by selective mutation of voltage sensor domain residues, have been investigated using classical molecular dynamics simulations. Following experiments that have identified mutations of voltage-gated ion channels involved in state-dependent omega currents, we observe for both the open and closed conformations of the Kv1.2 that specific mutations of S4 gating-charge residues destabilize the electrostatic network between helices of the voltage sensor domain, resulting in the formation of hydrophilic pathways linking the intra- and extracellular media. When such mutant channels are subject to transmembrane potentials, they conduct cations via these so-called omega pores. This study provides therefore further insight into the molecular mechanisms that lead to omega currents, which have been linked to certain channelopathies.
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