1ho7

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(New page: 200px<br /><applet load="1ho7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ho7" /> '''NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGM...)
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'''NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE'''<br />
'''NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1HO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HO7 OCA].
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1HO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO7 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gorlach, M.]]
[[Category: Gorlach, M.]]
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[[Category: Haris, P.I.]]
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[[Category: Haris, P I.]]
[[Category: Hojo, H.]]
[[Category: Hojo, H.]]
[[Category: Ohlenschlager, O.]]
[[Category: Ohlenschlager, O.]]
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[[Category: peptide]]
[[Category: peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:42:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:15 2008''

Revision as of 11:03, 21 February 2008


1ho7

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NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE

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

1HO7 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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