1ho2
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ho2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho2 OCA], [http://www.ebi.ac.uk/pdbsum/1ho2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ho2 RCSB]</span> | ||
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[[Category: amphipathic]] | [[Category: amphipathic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:13 2008'' |
Revision as of 18:08, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES
Overview
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.
About this Structure
1HO2 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel., Ohlenschlager O, Hojo H, Ramachandran R, Gorlach M, Haris PI, Biophys J. 2002 Jun;82(6):2995-3002. PMID:12023222
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