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PMID: 8552626 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Pérez-García MT, Chiamvimonvat N, Marban E, Tomaselli GF

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.

MeSH Terms
Amino Acid Sequence Animals Cadmium/pharmacology Cysteine/chemistry Ion Channel Gating/drug effects Molecular Sequence Data Mutagenesis, Site-Directed Oocytes Protein Structure, Secondary Rats Sodium Channels/chemistry,drug effects Structure-Activity Relationship Tetrodotoxin/pharmacology Xenopus laevis
Chemicals
Sodium Channels Cadmium Tetrodotoxin Cysteine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pérez-García M T
Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Chiamvimonvat N
Marban E
Tomaselli G F
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1996-01-09
Pages
300-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC40226
Subset
IM
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