Structure of the sodium channel pore revealed by serial cysteine mutagenesis.
- 9 January 1996
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 93 (1), 300-304
- https://doi.org/10.1073/pnas.93.1.300
Abstract
The pores of voltage-gated cation channels are formed by four intramembrane segments that impart selectivity and conductance. Remarkably little is known about the higher order structure of these critical pore-lining or P segments. Serial cysteine mutagenesis reveals a pattern of side-chain accessibility that contradicts currently favored structural models based on alpha-helices or beta-strands. Like the active sites of many enzymes of known structure, the sodium channel pore consists of irregular loop regions.Keywords
This publication has 33 references indexed in Scilit:
- Pore loops: An emerging theme in ion channel structureNeuron, 1995
- Silver as a Probe of Pore-Forming Residues in a Potassium ChannelScience, 1995
- Structural basis of ion channel permeation and selectivityCurrent Opinion in Neurobiology, 1994
- Differential contribution by conserved glutamate residues to an ion‐selectivity site in the L‐type Ca2+ channel poreFEBS Letters, 1993
- Molecular determinants of Ca2+ selectivity and ion permeation in L-type Ca2+ channelsNature, 1993
- Molecular Localization of an Ion-Binding Site Within the Pore of Mammalian Sodium ChannelsScience, 1992
- Calcium channel characteristics conferred on the sodium channel by single mutationsNature, 1992
- Mapping the site of block by tetrodotoxin and saxitoxin of sodium channel IIFEBS Letters, 1991
- Determination of the subunit stoichiometry of a voltage-activated potassium channelNature, 1991
- Pursuing the structure and function of voltage-gated channelsTrends in Neurosciences, 1990