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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
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/38358
Page Count: 5
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1996 National Academy of Sciences