Journal article
A Pore Segment in DEG/ENaC Na+Channels
The Journal of biological chemistry, Vol.274(40), pp.28484-28490
10/01/1999
DOI: 10.1074/jbc.274.40.28484
PMID: 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.
Details
- Title: Subtitle
- A Pore Segment in DEG/ENaC Na+Channels
- Creators
- Peter M SnyderDiane R OlsonDaniel B Bucher
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.274(40), pp.28484-28490
- DOI
- 10.1074/jbc.274.40.28484
- PMID
- 10497211
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Language
- English
- Date published
- 10/01/1999
- Academic Unit
- Molecular Physiology and Biophysics; Cardiovascular Medicine; Medicine Administration; Internal Medicine
- Record Identifier
- 9984025684602771
Metrics
26 Record Views