2A79
Mammalian Shaker Kv1.2 potassium channel- beta subunit complex
Summary for 2A79
Entry DOI | 10.2210/pdb2a79/pdb |
Related | 1EXB |
Descriptor | Voltage-gated potassium channel beta-2 subunit, Potassium voltage-gated channel subfamily A member 2, poly-unknown chain, ... (7 entities in total) |
Functional Keywords | potassium channel, voltage sensor, voltage dependent, ion channel, shaker, membrane protein, eukaryotic, kv1.2 |
Biological source | Rattus norvegicus (Norway rat) More |
Cellular location | Cytoplasm (Potential): P62483 Membrane; Multi-pass membrane protein: P63142 |
Total number of polymer chains | 4 |
Total formula weight | 101329.20 |
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 citation | Long, 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: 16002581DOI: 10.1126/science.1116269 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
