ArticleBiochemistry2014
Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- Dynamic protein-protein interactions of KCNQ1 and KCNE1 measured by EPR line shape analysis.Biochimica et biophysica acta. Biomembranes · 2024Article
- Non-canonical helical transitions and conformational switching are associated with characteristic flexibility and disorder indices in TRP and Kv channels.Channels (Austin, Tex.) · 2023Article
- The role of native cysteine residues in the oligomerization of KCNQ1 channels.Biochemical and biophysical research communications · 2023Article
- Modulation of the IBBA advances · 2023Article
- Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022Article
- Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing.Nature communications · 2020Article
- The membrane protein KCNQ1 potassium ion channel: Functional diversity and current structural insights.Biochimica et biophysica acta. Biomembranes · 2020Review
- Characterization of the Human KCNQ1 Voltage Sensing Domain (VSD) in Lipodisq Nanoparticles for Electron Paramagnetic Resonance (EPR) Spectroscopic Studies of Membrane Proteins.The journal of physical chemistry. B · 2020Article
- Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.eLife · 2020Article
- Genetic intolerance analysis as a tool for protein science.Biochimica et biophysica acta. Biomembranes · 2020Review
- CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.Journal of biomolecular NMR · 2019Article
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Article
- Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies.Chemistry and physics of lipids · 2019Article
- Phosphoinositide-interacting regulator of TRP (PIRT) has opposing effects on human and mouse TRPM8 ion channels.The Journal of biological chemistry · 2018Article
- Mechanisms of KCNQ1 channel dysfunction in long QT syndrome involving voltage sensor domain mutations.Science advances · 2018Article
- Peripheral myelin protein 22 alters membrane architecture.Science advances · 2017Article
- Regulation of KCNQ/Kv7 family voltage-gated KBiochimica et biophysica acta. Biomembranes · 2017Review
- Implications of Human Transient Receptor Potential Melastatin 8 (TRPM8) Channel Gating from Menthol Binding Studies of the Sensing Domain.Biochemistry · 2016Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
KCNQ1 (also known as KV7.1 or KVLQT1) is a voltage-gated potassium channel modulated by members of the KCNE protein family. Among multiple functions, KCNQ1 plays a critical role in the cardiac action potential. This channel is also subject to inherited mutations that cause certain cardiac arrhythmias and deafness. In this study, we report the overexpression, purification, and preliminary structural characterization of the voltage-sensor domain (VSD) of human KCNQ1 (Q1-VSD). Q1-VSD was expressed in Escherichia coli and purified into lyso-palmitoylphosphatidylglycerol micelles, conditions under which this tetraspan membrane protein yields excellent nuclear magnetic resonance (NMR) spectra. NMR studies reveal that Q1-VSD shares a common overall topology with other channel VSDs, with an S0 helix followed by transmembrane helices S1-S4. The exact sequential locations of the helical spans do, however, show significant variations from those of the homologous segments of previously characterized VSDs. The S4 segment of Q1-VSD was seen to be α-helical (with no 310 component) and underwent rapid backbone amide H-D exchange over most of its length. These results lay the foundation for more advanced structural studies and can be used to generate testable hypotheses for future structure-function experiments.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.