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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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Guda P,Bourne PE,Guda C

doi

10.1016/j.bbrc.2006.10.190

subject

Has Abstract

pub_date

2007-01-12 00:00:00

pages

292-8

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)02450-8

journal_volume

352

pub_type

杂志文章

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