Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment.

Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Research Abstract Details 

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Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Abstract Text:

Vishwanath Jogini, Roux,Vishwanath Jogini, Roux,

All-atom molecular dynamics simulations are used to better understand the dynamic environment experienced by the Kv1.2 channel in a lipid membrane. The structure of the channel is stable during the trajectories. The pore domain keeps a well-defined conformation, whereas the voltage-sensing domains undergo important lateral fluctuations, consistent with their modular nature. A channel-like region at the center of the S1-S4 helical bundle fills rapidly with water, reminiscent of the concept of high-dielectric aqueous crevices. The first two arginines along S4 (R294 and R297) adopt an interfacial position where they interact favorably with water and the lipid headgroups. The following two arginines (R300 and R303) interact predominantly with water and E226 in S2. Despite the absence of a structurally permanent gating pore formed by protein residues and surrounding the S4 helix, as traditionally pictured, the charged residues are located in a favorable environment and are not extensively exposed to the membrane nonpolar region. Continuum electrostatic computations indicate that the transmembrane potential sensed by the charged residues in the voltage sensor varies abruptly over the outer half of the membrane in the arginine-rich region of S4; thus, the voltage gradient or membrane electric field is "focused". Interactions of basic residues with the lipid headgroups at the intracellular membrane-solution interface reduce the membrane thickness near the channel, resulting in an increased transmembrane field.

Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Publishing Authors By Initials

V Jogini,B Roux,V Jogini,B Roux,

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Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Biophysical journal

VOLUME: 93

Page Numbers: 3070-82

Journal Abbreviation: Biophys. J.

ISSN: 0006-3495

DAY: 17

MONTH: 08

YEAR: 2007

Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Information

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LANGUAGE: eng

NlmUniqueID: 370626

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Grant and Affiliation Information for Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment.

AFFILIATION: Institute of Molecular Pediatric Sciences, Gordon Center for Integrative Science, The University of Chicago, Chicago, Illinois, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM062342

ACRONYM: GM

MEDLINETA: Biophys J

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