Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel
| Autor: | Lorie Thomas, Marco Colombini, Michael Forte, Elizabeth Blachly-Dyson |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1993 |
| Předmět: |
Voltage-dependent anion channel
Lipid Bilayers Molecular Sequence Data Analytical chemistry Porins Gating Saccharomyces cerevisiae Ion Channels Protein Structure Secondary Ion Voltage-Dependent Anion Channel 1 Voltage-Dependent Anion Channels Amino Acid Sequence Cloning Molecular Lipid bilayer Protein secondary structure Ion transporter Ion channel Multidisciplinary biology Chemistry Dextran Sulfate Electric Conductivity Membrane Proteins Recombinant Proteins Models Structural biology.protein Biophysics Mutagenesis Site-Directed Research Article |
| Popis: | Voltage-gated ion-channel proteins contain "voltage-sensing" domains that drive the conformational transitions between open and closed states in response to changes in transmembrane voltage. We have used site-directed mutagenesis to identify residues affecting the voltage sensitivity of a mitochondrial channel, the voltage-dependent anion-selective channel (VDAC). Although charge changes at many sites had no effect, at other sites substitutions that increased positive charge also increased the steepness of voltage dependence and substitutions that decreased positive charge decreased voltage dependence by an appropriate amount. In contrast to the plasma membrane K+ and Na+ channels, these residues are distributed over large parts of the VDAC protein. These results have been used to define the conformational transitions that accompany voltage gating of an ion channel. This gating mechanism requires the movement of large portions of the VDAC protein through the membrane. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|