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A Conserved Glutamate Is Important for Slow Inactivation in K + Channels

Voltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular end of segment 5 (S5) in slow inactivation by mutating it to a cysteine (E418C in Shaker). We could lock the channel in two different conforma... Full description

Journal Title: Neuron 2000, Vol.27 (3), p.573-583
Main Author: Larsson, H.Peter
Other Authors: Elinder, Fredrik
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States: Elsevier Inc
ID: ISSN: 0896-6273
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title: A Conserved Glutamate Is Important for Slow Inactivation in K + Channels
format: Article
creator:
  • Larsson, H.Peter
  • Elinder, Fredrik
subjects:
  • Amino Acid Sequence - genetics
  • Amino Acid Substitution
  • Animals
  • Barium - pharmacology
  • Conserved Sequence - genetics
  • Disulfides - chemistry
  • Glutamic Acid - genetics
  • Hydrogen Bonding
  • Hydrogen Peroxide - pharmacology
  • Ion Channel Gating - drug effects
  • Ion Channel Gating - genetics
  • Medical and Health Sciences
  • MEDICIN
  • Medicin och hälsovetenskap
  • MEDICINE
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Neuroscience(all)
  • Oocytes - cytology
  • Oocytes - metabolism
  • Patch-Clamp Techniques
  • Phenanthrolines - pharmacology
  • Potassium Channels - chemistry
  • Potassium Channels - genetics
  • Potassium Channels - metabolism
  • Protein Conformation - drug effects
  • Reducing Agents - pharmacology
  • Structure-Activity Relationship
  • Transfection
  • Xenopus
ispartof: Neuron, 2000, Vol.27 (3), p.573-583
description: Voltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular end of segment 5 (S5) in slow inactivation by mutating it to a cysteine (E418C in Shaker). We could lock the channel in two different conformations by disulfide-linking 418C to two different cysteines, introduced in the Pore–S6 (P–S6) loop. Our results suggest that E418 is normally stabilizing the open conformation of the slow inactivation gate by forming hydrogen bonds with the P–S6 loop. Breaking these bonds allows the P–S6 loop to rotate, which closes the slow inactivation gate. Our results also suggest a mechanism of how the movement of the voltage sensor can induce slow inactivation by destabilizing these bonds.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 0896-6273
fulltext: fulltext
issn:
  • 0896-6273
  • 1097-4199
  • 1097-4199
url: Link


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titleA Conserved Glutamate Is Important for Slow Inactivation in K + Channels
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descriptionVoltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular end of segment 5 (S5) in slow inactivation by mutating it to a cysteine (E418C in Shaker). We could lock the channel in two different conformations by disulfide-linking 418C to two different cysteines, introduced in the Pore–S6 (P–S6) loop. Our results suggest that E418 is normally stabilizing the open conformation of the slow inactivation gate by forming hydrogen bonds with the P–S6 loop. Breaking these bonds allows the P–S6 loop to rotate, which closes the slow inactivation gate. Our results also suggest a mechanism of how the movement of the voltage sensor can induce slow inactivation by destabilizing these bonds.
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subjectAmino Acid Sequence - genetics ; Amino Acid Substitution ; Animals ; Barium - pharmacology ; Conserved Sequence - genetics ; Disulfides - chemistry ; Glutamic Acid - genetics ; Hydrogen Bonding ; Hydrogen Peroxide - pharmacology ; Ion Channel Gating - drug effects ; Ion Channel Gating - genetics ; Medical and Health Sciences ; MEDICIN ; Medicin och hälsovetenskap ; MEDICINE ; Models, Molecular ; Mutagenesis, Site-Directed ; Neuroscience(all) ; Oocytes - cytology ; Oocytes - metabolism ; Patch-Clamp Techniques ; Phenanthrolines - pharmacology ; Potassium Channels - chemistry ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Protein Conformation - drug effects ; Reducing Agents - pharmacology ; Structure-Activity Relationship ; Transfection ; Xenopus
ispartofNeuron, 2000, Vol.27 (3), p.573-583
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descriptionVoltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular end of segment 5 (S5) in slow inactivation by mutating it to a cysteine (E418C in Shaker). We could lock the channel in two different conformations by disulfide-linking 418C to two different cysteines, introduced in the Pore–S6 (P–S6) loop. Our results suggest that E418 is normally stabilizing the open conformation of the slow inactivation gate by forming hydrogen bonds with the P–S6 loop. Breaking these bonds allows the P–S6 loop to rotate, which closes the slow inactivation gate. Our results also suggest a mechanism of how the movement of the voltage sensor can induce slow inactivation by destabilizing these bonds.
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1Amino Acid Substitution
2Animals
3Barium - pharmacology
4Conserved Sequence - genetics
5Disulfides - chemistry
6Glutamic Acid - genetics
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16Mutagenesis, Site-Directed
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22Potassium Channels - chemistry
23Potassium Channels - genetics
24Potassium Channels - metabolism
25Protein Conformation - drug effects
26Reducing Agents - pharmacology
27Structure-Activity Relationship
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6Glutamic Acid - genetics
7Hydrogen Bonding
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26Reducing Agents - pharmacology
27Structure-Activity Relationship
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abstractVoltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular end of segment 5 (S5) in slow inactivation by mutating it to a cysteine (E418C in Shaker). We could lock the channel in two different conformations by disulfide-linking 418C to two different cysteines, introduced in the Pore–S6 (P–S6) loop. Our results suggest that E418 is normally stabilizing the open conformation of the slow inactivation gate by forming hydrogen bonds with the P–S6 loop. Breaking these bonds allows the P–S6 loop to rotate, which closes the slow inactivation gate. Our results also suggest a mechanism of how the movement of the voltage sensor can induce slow inactivation by destabilizing these bonds.
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doi10.1016/S0896-6273(00)00067-2
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