Abstract
Voltage-gated ion channels are integral membrane proteins that mediate ion transport across membranes. KCNQ1 is a human voltage-gated potassium channel that is expressed in both epithelial and cardiac tissues. KCNQ1 associates with KCNE1 and mediates the Iks current responsible for the repolarization of the cardiac action potential. Mutations of KCNQ1 that cause a loss-of-function result in congenital long-QT syndrome (LQTS), which predisposes individuals to cardiac arrhythmia and can result in sudden death. We have previously described the high level expression and purification of the S1-S4 voltage sensor domain (VSD) of human KCNQ1 (Peng-D et al., Biochemistry53:2032-42, 2014). Here we describe the results of NMR-based structural studies of this protein and of efforts to map its drug binding sites. This work was supported by RO1 HL122010 and by F32 GM117770.
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