Abstract
KCNE3 is a single transmembrane protein that modulates the function and trafficking of several voltage-gated potassium channels, including KCNQ1, KCNQ4, hERG, Kv2.1, Kv3.1, and Kv3.2. KCNE3 binds with KCNQ1 and plays a crucial role in potassium ion recycling, which is important for transepithelial chloride ion secretion. Mutations in KCNE3 are linked to diseases associated with salt and fluid disorders including cystic fibrosis (CF). Despite the biological significance, structural and dynamic properties of KCNE3 is not fully understood in different membrane environment. In this study, we investigate structural and dynamic properties of KCNE3 in different membrane environments such as POPC, POPC/POPG, DMPC, DOPC, using molecular dynamics simulation. The amino acid locations and side chain dynamics of WT KCNE3 will be compared to the mutated form of KCNE3. The molecular dynamics simulation studies will be compared with the continuous wave electron paramagnetic resonance (CW-EPR) lineshape analysis results.
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