STRUCTURE OF THE SODIUM-CHANNEL PORE REVEALED BY SERIAL CYSTEINE MUTAGENESIS

Authors
PEREZGARCIA MT CHIAMVIMONVAT N MARBAN E TOMASELLI GF
Citation
Mt. Perezgarcia et al., STRUCTURE OF THE SODIUM-CHANNEL PORE REVEALED BY SERIAL CYSTEINE MUTAGENESIS, Proceedings of the National Academy of Sciences of the United Statesof America, 93(1), 1996, pp. 300-304
Citations number
37
Categorie Soggetti
Multidisciplinary Sciences
Journal title
Proceedings of the National Academy of Sciences of the United Statesof America → ACNP
ISSN journal
00278424
Volume
93
Issue
1
Year of publication
1996
Pages
300 - 304
Database
ISI
SICI code
0027-8424(1996)93:1<300:SOTSPR>2.0.ZU;2-3
Abstract
The pores of voltage-gated cation channels are formed by four intramem brane segments that impart selectivity and conductance, Remarkably lit tle is known about the higher order structure of these critical pore-l ining 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 o f irregular loop regions.