The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
The Cavity and Pore Helices in the KcsA K + Channel: Electrostatic Stabilization of Monovalent Cations
Abstract
The electrostatic influence of the central cavity and pore alpha helices in the potassium ion channel from Streptomyces lividans (KcsA K + channel) was analyzed by solving the finite difference Poisson equation. The cavity and helices overcome the destabilizing influence of the membrane and stabilize a cation at the membrane center. The electrostatic effect of the pore helices is large compared to that described for water-soluble proteins because of the low dielectric membrane environment. The combined contributions of the ion self-energy and the helix electrostatic field give rise to selectivity for monovalent cations in the water-filled cavity. Thus, the K + channel uses simple electrostatic principles to solve the fundamental problem of ion destabilization by the cell membrane lipid bilayer.
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Self-citationThe Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
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Cited by
Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution
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Self-citationX-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
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Self-citationEnergetics of ion conduction through the K+ channel
Bernèche, S., & Roux, B. (2001) · Nature · doi:10.1038/35102067 · Cited by 803
Self-citationCrystal Structure of the Potassium Channel KirBac1.1 in the Closed State
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Gating the Selectivity Filter in ClC Chloride Channels
Dutzler, R., Campbell, E. B., & MacKinnon, R. (2003) · Science · doi:10.1126/science.1082708 · Cited by 727
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Metadata
- Authors
- Roux, B., & MacKinnon, R.
- Venue
- Science
- Published
- 1999-07-02
- Volume
- 285
- Issue
- 5424
- Pages
- 100-102
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2076832064
- Cited by
- 434
- References
- 13
- FWCI
- 12.40
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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