Abenavoli, Alessandra ; DiFrancesco, Mattia Lorenzo ; Schroeder, Indra ; Epimashko, Svetlana ; Gazzarrini, Sabrina ; Hansen, Ulf Peter ; Thiel, Gerhard ; Moroni, Anna (2009)
Fast and slow gating are inherent properties of the pore module of the K+ channel Kcv.
In: The Journal of general physiology, 134 (3)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Kcv from the chlorella virus PBCV-1 is a viral protein that forms a tetrameric, functional K+ channel in heterologous systems. Kcv can serve as a model system to study and manipulate basic properties of the K+ channel pore because its minimalistic structure (94 amino acids) produces basic features of ion channels, such as selectivity, gating, and sensitivity to blockers. We present a characterization of Kcv properties at the single-channel level. In symmetric 100 mM K+, single-channel conductance is 114+/-11 pS. Two different voltage-dependent mechanisms are responsible for the gating of Kcv. "Fast" gating, analyzed by beta distributions, is responsible for the negative slope conductance in the single-channel current-voltage curve at extreme potentials, like in MaxiK potassium channels, and can be explained by depletion-aggravated instability of the filter region. The presence of a "slow" gating is revealed by the very low (in the order of 1-4%) mean open probability that is voltage dependent and underlies the time-dependent component of the macroscopic current.
Typ des Eintrags: | Artikel |
---|---|
Erschienen: | 2009 |
Autor(en): | Abenavoli, Alessandra ; DiFrancesco, Mattia Lorenzo ; Schroeder, Indra ; Epimashko, Svetlana ; Gazzarrini, Sabrina ; Hansen, Ulf Peter ; Thiel, Gerhard ; Moroni, Anna |
Art des Eintrags: | Bibliographie |
Titel: | Fast and slow gating are inherent properties of the pore module of the K+ channel Kcv. |
Sprache: | Englisch |
Publikationsjahr: | 2009 |
Titel der Zeitschrift, Zeitung oder Schriftenreihe: | The Journal of general physiology |
Jahrgang/Volume einer Zeitschrift: | 134 |
(Heft-)Nummer: | 3 |
Kurzbeschreibung (Abstract): | Kcv from the chlorella virus PBCV-1 is a viral protein that forms a tetrameric, functional K+ channel in heterologous systems. Kcv can serve as a model system to study and manipulate basic properties of the K+ channel pore because its minimalistic structure (94 amino acids) produces basic features of ion channels, such as selectivity, gating, and sensitivity to blockers. We present a characterization of Kcv properties at the single-channel level. In symmetric 100 mM K+, single-channel conductance is 114+/-11 pS. Two different voltage-dependent mechanisms are responsible for the gating of Kcv. "Fast" gating, analyzed by beta distributions, is responsible for the negative slope conductance in the single-channel current-voltage curve at extreme potentials, like in MaxiK potassium channels, and can be explained by depletion-aggravated instability of the filter region. The presence of a "slow" gating is revealed by the very low (in the order of 1-4%) mean open probability that is voltage dependent and underlies the time-dependent component of the macroscopic current. |
Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen) ?? fb10_botanik ?? 10 Fachbereich Biologie |
Hinterlegungsdatum: | 21 Jun 2011 11:59 |
Letzte Änderung: | 05 Mär 2013 09:49 |
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