Key result
The C-terminal domains of KCNQ1 and KCNE1 physically interact with a dissociation constant of ~4 microM, an association that may be affected by some long QT syndrome mutations.
Population
Cultured cells and purified KCNQ1-CT and KCNE1-CT proteins
Design
Preclinical
Authors
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May inform IKs channel models in long QT syndrome; leaves open therapeutic targeting pending human validation.
Effect estimate: dissociation constant ~4 microM
Demonstrates a direct physical interaction between the C-terminal domains of KCNQ1 and KCNE1, providing mechanistic insight into IKs channel regulation and the pathophysiology of some Long QT syndrome mutations.
Zheng et al. (2010) studied Long QT syndrome (context). KCNQ1-CT and KCNE1-CT interaction was evaluated on Physical interaction and binding affinity between KCNQ1-CT and KCNE1-CT (dissociation constant ~4 microM). The C-terminal domains of KCNQ1 and KCNE1 physically interact with a dissociation constant of ~4 microM, an association that may be affected by some long QT syndrome mutations.
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