Key result
Replacement of conserved cysteine residues C122 and C154 in the Kir2.1 channel abolished current and acted in a dominant-negative manner, suggesting an intramolecular disulfide bond is required for proper folding.
Population
Xenopus laevis oocytes expressing wild-type or mutant Kir2.1 channels
Comparison
Replacement of cysteine residues C122 and C154… vs Wild-type Kir2.1 channels
Design
Preclinical
Authors
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Highlights potential structural basis for Kir2.1 channelopathies; hypothesis-generating in animal models and needs human validation.
An intramolecular disulfide bond between C122 and C154 is essential for the proper folding and function of the Kir2.1 potassium channel.
Cho et al. (2000) studied Kir2.1 channel function. Mutation of C122 and C154 to alanine or serine vs. Wild-type Kir2.1 was evaluated on Channel current and folding. Replacement of conserved cysteine residues C122 and C154 in the Kir2.1 channel abolished current and acted in a dominant-negative manner, suggesting an intramolecular disulfide bond is required for proper folding.
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