PIP2 Binding at Allosteric Site Blocks Activation in Human Rod CNG Channels
Taehyun Park, Crina M. Nimigean
This study identifies how PIP2 binding at an allosteric site inhibits human rod CNG channels by stabilizing non-conductive conformations.
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Weill Cornell MedicineORCID 0000-0002-6254-4447Unclaimed ORCID profile · follow to get notified of new preprints
3 papers
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Taehyun Park, Crina M. Nimigean
This study identifies how PIP2 binding at an allosteric site inhibits human rod CNG channels by stabilizing non-conductive conformations.
Reinier de Vries, Hee-Seop Yoo, Chen Fan…·Bert L. de Groot
This study investigates the gating mechanism of MthK channels using mutants, revealing hydrophobic and lipid-mediated processes that drive channel closure.
Chieh-Chin Li, Crina M. Nimigean
This study identifies a salt bridge in the bacterial ion channel SthK that functions as a temperature sensor, with lipid composition modulating its sensitivity to temperature changes.