February 1, 1999Biochemistry

Electrostatic Mutations in Iberiotoxin as a Unique Tool for Probing the Electrostatic Structure of the Maxi-K Channel Outer Vestibule

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Structured PICO

Population

Single maxi-K channels incorporated into planar lipid bilayers

Intervention

Five mutants of Iberiotoxin (IbTX) at positions K27 and R34 (including K27N, K27Q, R34N, K27R)

Comparator

Wild-type Iberiotoxin

Outcome

Dissociation and association rate constants (koff and kon), and equilibrium dissociation constant (Kd)surrogate

Mutations in Iberiotoxin reveal that specific residues (K27 and R34) interact with the potassium binding site in the maxi-K channel pore, and that simple net charge does not solely control toxin ingress.

Discussion

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Implication

Identifies key IbTX residues for BK channel binding; leaves open whether these insights enable selective cardiovascular therapeutics.

Cite This Study

Mullmann et al. (1999) studied this question.

synapsesocial.com/papers/6a71504435aa2c282ce29ec0 https://doi.org/10.1021/bi982040+

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Electrostatic Mutations in Iberiotoxin as a Unique Tool for Probing the Electrostatic Structure of the Maxi-K Channel Outer Vestibule

Structured PICO

Discussion

Implication

Cite This Study

Electrostatic Mutations in Iberiotoxin as a Unique Tool for Probing the Electrostatic Structure of the Maxi-K Channel Outer Vestibule

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider