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. 1996 Jan 9;93(1):300–304. doi: 10.1073/pnas.93.1.300

Structure of the sodium channel pore revealed by serial cysteine mutagenesis.

M T Pérez-García 1, N Chiamvimonvat 1, E Marban 1, G F Tomaselli 1
PMCID: PMC40226  PMID: 8552626

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.

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Selected References

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