July 27, 2009Proceedings of the National Academy of SciencesOpen Access

A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels

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Population

N-truncated and long QT syndrome mutant (Y43A or R56Q) hERG potassium channels

Comparison

Reapplication of gene fragments encoding… vs Channels without the eag domain

Design

Preclinical

Authors

AGAhleah S. GustinaJohns Hopkins University MTMatthew C. TrudeauUniversity of Maryland, Baltimore

Discussion

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Implication

May inform eag-mimetic strategies for LQTS; leaves open translation from animal channels to patients.

Structured PICO

Population

N-truncated and long QT syndrome mutant (Y43A or R56Q) hERG potassium channels

Intervention

Reapplication of gene fragments encoding N-terminal residues 1-135 (the 'eag domain')

Comparator

Channels without the eag domain

Outcome

Restoration of regulation of deactivation gating and physical interactions (measured by FRET)surrogate

Direct, noncovalent interactions between the eag domain and the channel core regulate hERG deactivation gating, suggesting small molecules mimicking this domain could restore function in LQTS mutant channels.

Cite This Study

Gustina et al. (2009) studied this question.

synapsesocial.com/papers/6a83eeb0a3cef8348e997a27 https://doi.org/10.1073/pnas.0900180106

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A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels

Discussion

Member takes

Implication

Structured PICO

Cite This Study

A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider