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Structure of the Sodium Channel Pore Revealed by Serial Cysteine Mutagenesis

M. T. Pérez-García, N. Chiamvimonvat, E. Marban and G. F. Tomaselli
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 1 (Jan. 9, 1996), pp. 300-304
Stable URL: http://www.jstor.org/stable/38358
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Structure of the Sodium Channel Pore Revealed by Serial Cysteine Mutagenesis
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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 α -helices or β -strands. Like the active sites of many enzymes of known structure, the sodium channel pore consists of irregular loop regions.

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