1J95
KCSA potassium channel with TBA (tetrabutylammonium) and potassium
Summary for 1J95
| Entry DOI | 10.2210/pdb1j95/pdb |
| Related | 1BL8 |
| Descriptor | VOLTAGE-GATED POTASSIUM CHANNEL, POTASSIUM ION, TETRABUTYLAMMONIUM ION (3 entities in total) |
| Functional Keywords | membrane protein, metal transport |
| Biological source | Streptomyces lividans |
| Cellular location | Cell membrane; Multi-pass membrane protein: P0A334 |
| Total number of polymer chains | 4 |
| Total formula weight | 53938.02 |
| Authors | Morais-Cabral, J.H.,MacKinnon, R.,Zhou, M. (deposition date: 2001-05-23, release date: 2001-06-13, Last modification date: 2023-08-16) |
| Primary citation | Zhou, M.,Morais-Cabral, J.H.,Mann, S.,MacKinnon, R. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors Nature, 411:657-661, 2001 Cited by PubMed Abstract: Many voltage-dependent K+ channels open when the membrane is depolarized and then rapidly close by a process called inactivation. Neurons use inactivating K+ channels to modulate their firing frequency. In Shaker-type K+ channels, the inactivation gate, which is responsible for the closing of the channel, is formed by the channel's cytoplasmic amino terminus. Here we show that the central cavity and inner pore of the K+ channel form the receptor site for both the inactivation gate and small-molecule inhibitors. We propose that inactivation occurs by a sequential reaction in which the gate binds initially to the cytoplasmic channel surface and then enters the pore as an extended peptide. This mechanism accounts for the functional properties of K+ channel inactivation and indicates that the cavity may be the site of action for certain drugs that alter cation channel function. PubMed: 11395760DOI: 10.1038/35079500 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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