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Origin of functional diversity among tetrameric voltage-gated channels (Articolo in rivista)
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- Origin of functional diversity among tetrameric voltage-gated channels (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Alternative label
Anselmi, C; Carloni, P; Torre, V (2007)
Origin of functional diversity among tetrameric voltage-gated channels
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- Anselmi, C; Carloni, P; Torre, V (literal)
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- INFM, DEMOCRITOS Modelling Ctr Res Atomist Simulat, I-34014 Trieste, Italy; Scuola Int Super Studi Avanzati, SISSA, I-34014 Trieste, Italy (literal)
- Titolo
- Origin of functional diversity among tetrameric voltage-gated channels (literal)
- Abstract
- The aim of the present work is to relate functional differences of voltage-gated K+ (K-v), hyperpolarization-activated cyclic nucleotide-gated (HCN), and cyclic nucleotide gated (CNG) channels to differences in their amino acid sequences. By means of combined bioinformatic sequence analyses and homology modelling, we suggest that: (1) CNG channels are less voltage-dependent than K-v channels since the charge of their voltage sensor, the S4 helix, is lower than that of K-v channels and because of the presence of a conserved proline in the S4-S5 linker, which is quite likely to uncouple S4 from S5 and S6. (2) In HCN channels, S4 features a higher net positive charge with respect to Kv channels and an extensive network of hydrophobic residues, which is quite likely to provide a tight coupling among S4 and the neighboring helices. We suggest insights on the gating of HCN channels and the reasons why they open with membrane hyperpolarization and with a significantly longer time constant with respect to other channels. Proteins 2007;66:136-146. (c) 2006 Wiley-Liss, Inc. (literal)
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