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Biochem Biophys Res Commun. 2007 Jan 12;352(2):292-8. Epub 2006 Nov 13.

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

Author information

1
GenNYsis Center for Excellence in Cancer Genomics and Department of Epidemiology and Biostatistics, State University of New York at Albany, One Discovery Drive, Rensselaer, NY 12144-3456, USA. cguda@albany.edu

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.

PMID:
17126810
DOI:
10.1016/j.bbrc.2006.10.190
[Indexed for MEDLINE]

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