日本語
 
Help Privacy Policy ポリシー/免責事項
  詳細検索ブラウズ

アイテム詳細


公開

学術論文

A novel Conus peptide ligand for K+ channels

MPS-Authors
/persons/resource/persons182147

Ferber,  Michael
Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society;

/persons/resource/persons182424

Sporning,  Annett
Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society;

/persons/resource/persons15918

Terlau,  Heinrich
Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society;

External Resource
There are no locators available
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
フルテキスト (公開)
公開されているフルテキストはありません
付随資料 (公開)
There is no public supplementary material available
引用

Ferber, M., Sporning, A., Jeserich, G., DeLaCruz, R., Watkins, M., Olivera, B. M., & Terlau, H. (2003). A novel Conus peptide ligand for K+ channels. The Journal of Biological Chemistry, 278(4), 2177-2183.


引用: https://hdl.handle.net/11858/00-001M-0000-0029-2704-0
要旨
Voltage-gated ion channels determine the membrane excitability of cells. Although many Conus peptides that interact with voltage-gated Na+ and Ca2+ channels have been characterized, relatively few have been identified that interact with K+ channels. We describe a novel Conus peptide that interacts with the Shaker K+ channel, M-kappa-conotoxin RIIIK from Conus radiatus. The peptide was chemically synthesized. Although M- kappa-conotoxin RIIIK is structurally similar to the mu- conotoxins that are sodium channel blockers, it does not affect any of the sodium channels tested, but blocks Shaker K+ channels. Studies using Shaker K+ channel mutants with single residue substitutions reveal that the peptide interacts with the pore region of the channel. Introduction of a negative charge at residue 427 (K427D) greatly increases the affinity of the toxin, whereas the substitutions at two other residues, Phe(425) and Thr (449), drastically reduced toxin affinity. Based on the Shaker results, a teleost homolog of the Shaker K+ channel, TSha1 was identified as a M-kappa-conotoxin RIIIK target. Binding of M-kappa-conotoxin RIIIK is state-dependent, with an IC50 of 20 nM for the closed state and 60 nm at 0 mV for the open state of TSha1 channels.