Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2A79

Mammalian Shaker Kv1.2 potassium channel- beta subunit complex

Summary for 2A79
Entry DOI10.2210/pdb2a79/pdb
Related1EXB
DescriptorVoltage-gated potassium channel beta-2 subunit, Potassium voltage-gated channel subfamily A member 2, poly-unknown chain, ... (7 entities in total)
Functional Keywordspotassium channel, voltage sensor, voltage dependent, ion channel, shaker, membrane protein, eukaryotic, kv1.2
Biological sourceRattus norvegicus (Norway rat)
More
Cellular locationCytoplasm (Potential): P62483
Membrane; Multi-pass membrane protein: P63142
Total number of polymer chains4
Total formula weight101329.20
Authors
Long, S.B.,Campbell, E.B.,MacKinnon, R. (deposition date: 2005-07-05, release date: 2005-07-12, Last modification date: 2023-08-23)
Primary citationLong, S.B.,Campbell, E.B.,Mackinnon, R.
Crystal structure of a mammalian voltage-dependent Shaker family K+ channel.
Science, 309:897-903, 2005
Cited by
PubMed Abstract: Voltage-dependent potassium ion (K+) channels (Kv channels) conduct K+ ions across the cell membrane in response to changes in the membrane voltage, thereby regulating neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal structure, at a resolution of 2.9 angstroms, of a mammalian Kv channel, Kv1.2, which is a member of the Shaker K+ channel family. This structure is in complex with an oxido-reductase beta subunit of the kind that can regulate mammalian Kv channels in their native cell environment. The activation gate of the pore is open. Large side portals communicate between the pore and the cytoplasm. Electrostatic properties of the side portals and positions of the T1 domain and beta subunit are consistent with electrophysiological studies of inactivation gating and with the possibility of K+ channel regulation by the beta subunit.
PubMed: 16002581
DOI: 10.1126/science.1116269
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon