Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins

Purnima Guda, Philip E. Bourne, Chittibabu Guda

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Voltage-gated ion channels (VGCs) mediate selective diffusion of ions across cell membranes to enable many vital cellular processes. Three-dimensional structure data are lacking for VGC proteins; hence, to better understand their function, there is a need to identify the conserved motifs using sequence analysis methods. In this study, we have used a profile-to-profile alignment method to identify several new conserved motifs specific to each transmembrane segment (TMS) of the voltage-sensing and the pore-forming modules of Ca2+, Na+, and K+ channel subfamilies. For Ca2+ and Na+, the functional theme of motif conservation is similar in all segments while they differ with those of the K+ channel proteins. Nevertheless, the conservation is strikingly similar in the S4 segment of the voltage-sensing module across all subfamilies. In each subfamily and for each TMS, we have identified conserved motifs/residues and correlated their functional significance and disease associations in human, using mutational data from the literature.

Original languageEnglish (US)
Pages (from-to)292-298
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume352
Issue number2
DOIs
StatePublished - Jan 12 2007

Keywords

  • Calcium channel proteins
  • Potassium channel proteins
  • Profile-to-profile alignment
  • Sodium channel proteins
  • VGC motifs
  • VGC proteins
  • Voltage-gated ion channel proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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