Article
Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.
Proceedings of the National Academy of Sciences of the United States of America - 31 Mar 2020
Sun Zhiyu, Xu Yunyao, Zhang Dongyu, McDermott Ann E
Abstract excerpt
Transmembrane allosteric coupling is a feature of many critical biological signaling events. Here we test whether transmembrane allosteric coupling controls the potassium binding affinity of the prototypical potassium channel KcsA in the context of C-type inactivation. Activation of KcsA is initiated by proton binding to the pH gate upon an intracellular drop in pH. Numerous studies have suggested that this...
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