Key result
Mutagenesis of the KcsA K+ channel identified two mutants, A108S and A108T, which dramatically increased open probability while retaining oligomeric stability.
Population
KcsA K+ channel in TK2420 Escherichia coli strain
Design
Preclinical
Authors
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No immediate clinical implications; leaves open translation of KcsA mutants to mammalian channels or therapies.
Mutagenesis of the KcsA K+ channel identified A108S and A108T mutants with increased open probability, providing insights into channel gating mechanisms.
Irizarry et al. (2002) studied this question. Tryptophan scanning and random mutagenesis was evaluated on Oligomeric stability and ability to complement K+ uptake deficiency. Mutagenesis of the KcsA K+ channel identified two mutants, A108S and A108T, which dramatically increased open probability while retaining oligomeric stability.
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