September 1, 2001Biochemistry

Binding of Correolide to the Kv1.3 Potassium Channel: Characterization of the Binding Domain by Site-Directed Mutagenesis

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Population

Membranes expressing homotetrameric K(v)1.3 channels and site-directed mutants along S(5) and S(6)

Design

Preclinical

Authors

MHMarkus HannerVienna Biocenter BGBrian GreenAID Atlanta YGYing‐Duo GaoCapital Institute of Pediatrics

Discussion

Member takes

Implication

May guide Kv1.3 modulator design but should not change practice; leaves open human validation.

Structured PICO

Population

Membranes expressing homotetrameric K(v)1.3 channels and site-directed mutants along S(5) and S(6)

Intervention

[(3)H]Dihydrocorreolide (diTC) binding

Outcome

Identification of residues contributing to high affinity binding of diTC

Site-directed mutagenesis and molecular modeling reveal that diTC binds in the water-filled cavity below the selectivity filter of the Kv1.3 channel, interacting with specific residues in S5 and S6.

Cite This Study

Hanner et al. (2001) studied this question.

synapsesocial.com/papers/6a7da3390210b8d50ccda3fd https://doi.org/10.1021/bi0111698

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Binding of Correolide to the Kv1.3 Potassium Channel: Characterization of the Binding Domain by Site-Directed Mutagenesis

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Binding of Correolide to the Kv1.3 Potassium Channel: Characterization of the Binding Domain by Site-Directed Mutagenesis

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider