Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer.

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Research Abstract Details 

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Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Abstract Text:

Jessica Richardson,Rikard Blunck,Pinghua Ge,Paul R Selvin,Francisco Bezanilla,Diane M Papazian,Ana M Correa,

Voltage-dependent ion channels are fundamental to the physiology of excitable cells because they underlie the generation and propagation of the action potential and excitation-contraction coupling. To understand how ion channels work, it is important to determine their structures in different conformations in a membrane environment. The validity of the crystal structure for the prokaryotic K(+) channel, K(V)AP, has been questioned based on discrepancies with biophysical data from functional eukaryotic channels, underlining the need for independent structural data under native conditions. We investigated the structural organization of two prokaryotic voltage-gated channels, NaChBac and K(V)AP, in liposomes by using luminescence resonance energy transfer. We describe here a transmembrane packing representation of the voltage sensor and pore domains of the prokaryotic Na channel, NaChBac. We find that NaChBac and K(V)AP share a common arrangement in which the structures of the Na and K selective pores and voltage-sensor domains are conserved. The packing arrangement of the voltage-sensing region as determined by luminescence resonance energy transfer differs significantly from that of the K(V)AP crystal structure, but resembles that of the eukaryotic K(V)1.2 crystal structure. However, the voltage-sensor domain in prokaryotic channels is closer to the pore domain than in the K(V)1.2 structure. Our results indicate that prokaryotic and eukaryotic channels that share similar functional properties have similar helix arrangements, with differences arising likely from the later introduction of additional structural elements.

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Publishing Authors By Initials

J Richardson,R Blunck,P Ge,PR Selvin,F Bezanilla,DM Papazian,AM Correa,

For similar proteins: carrier proteins: membrane transport proteins: ion channels: sodium channels research abstracts see: proteins: carrier proteins: membrane transport proteins: ion channels: sodium channels research

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Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 103

Page Numbers: 15865-70

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 16

MONTH: 10

YEAR: 2006

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7505876

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Keywords Mesh Terms:

KEYWORDS: Sodium Channels

MESH TERMS: metabolism

Chemical & Substance for Abstract: Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer. Information

Substance Name: Sodium Channels

Registry Number: 0

Grant and Affiliation Information for Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer.

AFFILIATION: Departments of Anesthesiology and *Physiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM74770

ACRONYM: GM

MEDLINETA: Proc Natl Acad Sci U S A

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