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

12 Citations (Scopus)

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

Fingerprint

Ion Channels
Electric potential
Sequence Analysis
Conservation
Proteins
Cell Membrane
Ions
Cell membranes
protein K

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

Cite this

Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins. / Guda, Purnima; Bourne, Philip E.; Guda, Chittibabu.

In: Biochemical and Biophysical Research Communications, Vol. 352, No. 2, 12.01.2007, p. 292-298.

Research output: Contribution to journalArticle

@article{47735ddb444947a69c06915f1e0a2de9,
title = "Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins",
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.",
keywords = "Calcium channel proteins, Potassium channel proteins, Profile-to-profile alignment, Sodium channel proteins, VGC motifs, VGC proteins, Voltage-gated ion channel proteins",
author = "Purnima Guda and Bourne, {Philip E.} and Chittibabu Guda",
year = "2007",
month = "1",
day = "12",
doi = "10.1016/j.bbrc.2006.10.190",
language = "English (US)",
volume = "352",
pages = "292--298",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins

AU - Guda, Purnima

AU - Bourne, Philip E.

AU - Guda, Chittibabu

PY - 2007/1/12

Y1 - 2007/1/12

N2 - 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.

AB - 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.

KW - Calcium channel proteins

KW - Potassium channel proteins

KW - Profile-to-profile alignment

KW - Sodium channel proteins

KW - VGC motifs

KW - VGC proteins

KW - Voltage-gated ion channel proteins

UR - http://www.scopus.com/inward/record.url?scp=33751531559&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33751531559&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2006.10.190

DO - 10.1016/j.bbrc.2006.10.190

M3 - Article

C2 - 17126810

AN - SCOPUS:33751531559

VL - 352

SP - 292

EP - 298

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -