Structure of the sodium channel pore revealed by serial cysteine mutagenesis

M. T. Pérez-García, N. Chiamvimonvat, E. Marban, Gordon F. Tomaselli

Research output: Contribution to journalArticle

105 Citations (Scopus)

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 pure- 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.

Original languageEnglish (US)
Pages (from-to)300-304
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number1
DOIs
StatePublished - Jan 9 1996
Externally publishedYes

Fingerprint

Sodium Channels
Structural Models
Mutagenesis
Cysteine
Cations
Catalytic Domain
Enzymes

ASJC Scopus subject areas

  • General

Cite this

Structure of the sodium channel pore revealed by serial cysteine mutagenesis. / Pérez-García, M. T.; Chiamvimonvat, N.; Marban, E.; Tomaselli, Gordon F.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, No. 1, 09.01.1996, p. 300-304.

Research output: Contribution to journalArticle

@article{411fcba2f811498cb13f544b7cc61cc3,
title = "Structure of the sodium channel pore revealed by serial cysteine mutagenesis",
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 pure- 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.",
author = "P{\'e}rez-Garc{\'i}a, {M. T.} and N. Chiamvimonvat and E. Marban and Tomaselli, {Gordon F.}",
year = "1996",
month = "1",
day = "9",
doi = "10.1073/pnas.93.1.300",
language = "English (US)",
volume = "93",
pages = "300--304",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "1",

}

TY - JOUR

T1 - Structure of the sodium channel pore revealed by serial cysteine mutagenesis

AU - Pérez-García, M. T.

AU - Chiamvimonvat, N.

AU - Marban, E.

AU - Tomaselli, Gordon F.

PY - 1996/1/9

Y1 - 1996/1/9

N2 - 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 pure- 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.

AB - 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 pure- 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.

UR - http://www.scopus.com/inward/record.url?scp=0030051135&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030051135&partnerID=8YFLogxK

U2 - 10.1073/pnas.93.1.300

DO - 10.1073/pnas.93.1.300

M3 - Article

VL - 93

SP - 300

EP - 304

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 1

ER -