2JK5
Potassium Channel KcsA in complex with Tetrabutylammonium in high K
Summary for 2JK5
| Entry DOI | 10.2210/pdb2jk5/pdb |
| Related | 1BL8 1F6G 1J95 1JQ1 1JQ2 1JVM 1K4C 1K4D 1R3I 1R3J 1R3K 1R3L 1ZWI 2A9H 2ATK 2BOB 2BOC 2H8P 2HG5 2IH1 2IH3 2W0F 4UUJ |
| Descriptor | ANTIBODY FAB FRAGMENT LIGHT CHAIN, ANTIBODY FAB FRAGMENT HEAVY CHAIN, VOLTAGE-GATED POTASSIUM CHANNEL, ... (10 entities in total) |
| Functional Keywords | immune system-metal transport complex, quaternary ammonium, protein-antibody fab complex, ionic channel, ion transport, immune system/metal transport |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: 2JK5 |
| Total number of polymer chains | 3 |
| Total formula weight | 61279.66 |
| Authors | Lenaeus, M.J.,Focia, P.J.,Wagner, T.,Gross, A. (deposition date: 2008-08-15, release date: 2009-11-17, Last modification date: 2024-10-23) |
| Primary citation | Lenaeus, M.J.,Burdette, D.,Wagner, T.,Focia, P.J.,Gross, A. Structures of Kcsa in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site. Biochemistry, 53:5365-, 2014 Cited by PubMed Abstract: Potassium channels allow for the passive movement of potassium ions across the cell membrane and are instrumental in controlling the membrane potential in all cell types. Quaternary ammonium (QA) compounds block potassium channels and have long been used to study the functional and structural properties of these channels. Here we describe the interaction between three symmetrical hydrophobic QAs and the prokaryotic potassium channel KcsA. The structures demonstrate the presence of a hydrophobic pocket between the inner helices of KcsA and provide insight into the binding site and blocking mechanism of hydrophobic QAs. The structures also reveal a structurally hidden pathway between the central cavity and the outside membrane environment reminiscent of the lateral fenestration observed in sodium channels that can be accessed through small conformational changes in the pore wall. We propose that the hydrophobic binding pocket stabilizes the alkyl chains of long-chain QA molecules and may play a key role in hydrophobic drug binding in general. PubMed: 25093676DOI: 10.1021/BI500525S PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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