Referenced in: none

Automatically associated channels: Kv10.1

Title: A pore segment in DEG/ENaC Na(+) channels.

Authors: P M Snyder, D R Olson, D B Bucher

Journal, date & volume: J. Biol. Chem., 1999 Oct 1 , 274, 28484-90

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/10497211

Abstract
DEG/ENaC Na(+) channels have diverse functions, including Na(+) absorption, neurotransmission, and sensory transduction. The ability of these channels to discriminate between different ions is critical for their normal function. Several findings suggest that DEG/ENaC channels have a pore structure similar to K(+) channels. To test this hypothesis, we examined the accessibility of native and introduced cysteines in the putative P loop of ENaC. We identified residues that span a barrier that excludes amiloride as well as anionic and large methanethiosulfonate reagents from the pore. This segment contains a structural element ((S/G)CS) involved in selectivity of ENaC. The results are not consistent with predictions from the K(+) channel pore, suggesting that DEG/ENaC Na(+) channels have a novel pore structure.