September 17, 2014Journal of Biological ChemistryOpen Access

Modulation of the Voltage-gated Potassium Channel (Kv4.3) and the Auxiliary Protein (KChIP3) Interactions by the Current Activator NS5806

View Full Paper

Ask AI

Bookmark

Population

Recombinant mouse KChIP3 proteins and Kv4.3 peptide fragments (in vitro model)

Design

Preclinical

Authors

WGWalter G. GonzalezHalliburton (United Kingdom)KPKhoa PhamAlbert Einstein College of Medicine JMJaroslava MikšovskáFlorida International University

Discussion

Member takes

Implication

Supports NS5806 mechanism on Kv4.3; hypothesis-generating for cardiac ion channel therapies, needs in vivo validation.

Structured PICO

Population

Recombinant mouse KChIP3 proteins and Kv4.3 peptide fragments (in vitro model)

Intervention

NS5806 (potassium current activator)

Outcome

Binding affinity (Kd) and dissociation rates between KChIP3, Kv4.3, and NS5806surrogate

NS5806 directly interacts with KChIP3 to modulate its association with the Kv4.3 channel, providing a molecular mechanism for its potassium current activating properties which could inform drug design for heart conditions.

Limitations

Low solubility of the full T1 domain prevented further characterization of NS5806 binding directly at the T1 domain

Cite This Study

Gonzalez et al. (2014) studied this question.

synapsesocial.com/papers/6a8a585741f4089922bd92be https://doi.org/10.1074/jbc.m114.577528

View Full Paper

Ask AI

Bookmark

Modulation of the Voltage-gated Potassium Channel (Kv4.3) and the Auxiliary Protein (KChIP3) Interactions by the Current Activator NS5806

Discussion

Member takes

Implication

Structured PICO

Limitations

Cite This Study

Modulation of the Voltage-gated Potassium Channel (Kv4.3) and the Auxiliary Protein (KChIP3) Interactions by the Current Activator NS5806

Discussion

Member takes

Implication

Structured PICO

Limitations

Cite This Study

Also Consider

Also Consider