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The principle of gating charge movement in a voltage-dependent K+ channel.
- Source :
-
Nature [Nature] 2003 May 01; Vol. 423 (6935), pp. 42-8. - Publication Year :
- 2003
-
Abstract
- The steep dependence of channel opening on membrane voltage allows voltage-dependent K+ channels to turn on almost like a switch. Opening is driven by the movement of gating charges that originate from arginine residues on helical S4 segments of the protein. Each S4 segment forms half of a 'voltage-sensor paddle' on the channel's outer perimeter. Here we show that the voltage-sensor paddles are positioned inside the membrane, near the intracellular surface, when the channel is closed, and that the paddles move a large distance across the membrane from inside to outside when the channel opens. KvAP channels were reconstituted into planar lipid membranes and studied using monoclonal Fab fragments, a voltage-sensor toxin, and avidin binding to tethered biotin. Our findings lead us to conclude that the voltage-sensor paddles operate somewhat like hydrophobic cations attached to levers, enabling the membrane electric field to open and close the pore.
- Subjects :
- Amino Acid Sequence
Antibodies, Monoclonal immunology
Archaeal Proteins chemistry
Archaeal Proteins immunology
Archaeal Proteins metabolism
Avidin metabolism
Biotin metabolism
Desulfurococcaceae chemistry
Desulfurococcaceae metabolism
Hydrophobic and Hydrophilic Interactions
Immunoglobulin Fab Fragments immunology
Models, Biological
Models, Molecular
Molecular Sequence Data
Motion
Potassium Channels, Voltage-Gated antagonists & inhibitors
Potassium Channels, Voltage-Gated immunology
Protein Structure, Tertiary
Static Electricity
Structure-Activity Relationship
Ion Channel Gating
Potassium Channels, Voltage-Gated chemistry
Potassium Channels, Voltage-Gated metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 423
- Issue :
- 6935
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 12721619
- Full Text :
- https://doi.org/10.1038/nature01581