1orq
X-ray structure of a voltage-dependent potassium channel in complex with an Fab
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| , resolution 3.20Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1ORS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Voltage-dependent K+ channels are members of the family of voltage-dependent cation (K+, Na+ and Ca2+) channels that open and allow ion conduction in response to changes in cell membrane voltage. This form of gating underlies the generation of nerve and muscle action potentials, among other processes. Here we present the structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix. We have determined a crystal structure of the full-length channel at a resolution of 3.2 A, and of the isolated voltage-sensor domain at 1.9 A, both in complex with monoclonal Fab fragments. The channel contains a central ion-conduction pore surrounded by voltage sensors, which form what we call 'voltage-sensor paddles'-hydrophobic, cationic, helix-turn-helix structures on the channel's outer perimeter. Flexible hinges suggest that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane.
About this StructureAbout this Structure
1ORQ is a Protein complex structure of sequences from Aeropyrum pernix and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of a voltage-dependent K+ channel., Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, MacKinnon R, Nature. 2003 May 1;423(6935):33-41. PMID:12721618
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