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. 2002 Jun;82(6):2995–3002. doi: 10.1016/S0006-3495(02)75640-3

Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel.

Oliver Ohlenschläger 1, Hironobu Hojo 1, Ramadurai Ramachandran 1, Matthias Görlach 1, Parvez I Haris 1
PMCID: PMC1302087  PMID: 12023222

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.

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Selected References

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