2R9R

Shaker family voltage dependent potassium channel (kv1.2-kv2.1 paddle chimera channel) in association with beta subunit

Summary for 2R9R

• Entry DOI: 10.2210/pdb2r9r/pdb
• Related: 2a79
• Descriptor: Voltage-gated potassium channel subunit beta-2, Paddle chimera voltage gated potassium channel Kv1.2-Kv2.1, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• Functional Keywords: potassium channel, voltage sensor, voltage dependent, ion channel, shaker, membrane protein, eukaryotic, kv1.2, kv2.1, paddle chimera channel, ion transport, ionic channel, nadp, phosphorylation, potassium transport, transport, voltage-gated channel, protein transport, transport protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm (Potential): P62483
• Total number of polymer chains: 4
• Total formula weight: 206882.23

Authors

Long, S.B.,Tao, X.,Campbell, E.B.,Mackinnon, R. (deposition date: 2007-09-13, release date: 2007-11-20, Last modification date: 2023-08-30)

Primary citation

Long, S.B.,Tao, X.,Campbell, E.B.,MacKinnon, R.
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
Nature, 450:376-382, 2007

PubMed Abstract: Voltage-dependent K+ (Kv) channels repolarize the action potential in neurons and muscle. This type of channel is gated directly by membrane voltage through protein domains known as voltage sensors, which are molecular voltmeters that read the membrane voltage and regulate the pore. Here we describe the structure of a chimaeric voltage-dependent K+ channel, which we call the 'paddle-chimaera channel', in which the voltage-sensor paddle has been transferred from Kv2.1 to Kv1.2. Crystallized in complex with lipids, the complete structure at 2.4 ångström resolution reveals the pore and voltage sensors embedded in a membrane-like arrangement of lipid molecules. The detailed structure, which can be compared directly to a large body of functional data, explains charge stabilization within the membrane and suggests a mechanism for voltage-sensor movements and pore gating.

PubMed: 18004376
DOI: 10.1038/nature06265

Experimental method

X-RAY DIFFRACTION (2.4 Å)