Cysteine mutagenesis in the voltage-dependent sodium channel: Structural insights and implications

Gordon F. Tomaselli

Research output: Contribution to journalArticle

Abstract

The superfamily of ion channel proteins comprise multisubunit transmembrane glycoproteins that are the fundamental electrical signaling molecules in the heart and other excitable tissues. The large size and hydrophobicity of these proteins present a formidable obstacle to the generation of a crystal structure. In lieu of a high-resolution structure, complementary methods have been used to study the structure function relationships of these essential excitability proteins. Molecular cloning and biophysical analysis of heterologously expressed wild-type and mutant channel proteins have provided insights into the structural basis of the essential channel functions of permeation and gating. This powerful combination of techniques also provides dynamic structural information regarding channel proteins not likely to be forthcoming from a crystal structure.

Original languageEnglish (US)
Pages (from-to)211-218
Number of pages8
JournalTrends in Cardiovascular Medicine
Volume7
Issue number6
DOIs
StatePublished - 1997

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Sodium Channels
Mutagenesis
Cysteine
Proteins
Molecular Cloning
Mutant Proteins
Hydrophobic and Hydrophilic Interactions
Ion Channels
Glycoproteins

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine

Cite this

Cysteine mutagenesis in the voltage-dependent sodium channel : Structural insights and implications. / Tomaselli, Gordon F.

In: Trends in Cardiovascular Medicine, Vol. 7, No. 6, 1997, p. 211-218.

Research output: Contribution to journalArticle

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