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 language | English (US) |
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Pages (from-to) | 292-298 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 352 |
Issue number | 2 |
DOIs | |
State | Published - Jan 12 2007 |
Externally published | Yes |
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