1HO2
NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES
Summary for 1HO2
| Entry DOI | 10.2210/pdb1ho2/pdb |
| Descriptor | VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN (1 entity in total) |
| Functional Keywords | alpha-helix, amphipathic, membrane protein |
| Biological source | Drosophila melanogaster (fruit fly) |
| Cellular location | Membrane; Multi-pass membrane protein: P08510 |
| Total number of polymer chains | 1 |
| Total formula weight | 2200.63 |
| Authors | Ohlenschlager, O.,Hojo, H.,Ramachandran, R.,Gorlach, M.,Haris, P.I. (deposition date: 2000-12-08, release date: 2002-06-05, Last modification date: 2024-05-22) |
| Primary citation | Ohlenschlager, O.,Hojo, H.,Ramachandran, R.,Gorlach, M.,Haris, P.I. Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel. Biophys.J., 82:2995-3002, 2002 Cited by PubMed Abstract: The propagation of action potentials during neuronal signal transduction in phospholipid membranes is mediated by ion channels, a diverse group of membrane proteins. The S4-S5 linker peptide (S4-S5), that connects the S4 and S5 transmembrane segments of voltage-gated potassium channels is an important region of the Shaker ion-channel protein. Despite its importance, very little is known about its structure. Here we provide evidence for an amphipathic alpha-helical conformation of a synthetic S4-S5 peptide of the voltage-gated Drosophila melanogaster Shaker potassium channel in water/trifluoroethanol and in aqueous phospholipid micelles. The three-dimensional solution structures of the S4-S5 peptide were obtained by high-resolution nuclear magnetic resonance spectroscopy and distance-geometry/simulated-annealing calculations. The detailed structural features are discussed with respect to model studies and available mutagenesis data on the mechanism and selectivity of the potassium channel. PubMed: 12023222PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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