Related ArticlesInsights into hERG K+ channel structure and function from NMR studies.
Eur Biophys J. 2013 Jan;42(1):71-9
Authors: Ng CA, Torres AM, Pagès G, Kuchel PW, Vandenberg JI
Abstract
The unique gating kinetics of hERG K(+) channels are critical for normal cardiac repolarization, and patients with mutations in hERG have a markedly increased risk of cardiac arrhythmias and sudden cardiac arrest. HERG K(+) channels are also remarkably promiscuous with respect to drug binding, which has been a very significant problem for the pharmaceutical industry. Here, we review the progress that has been made in understanding the structure and function of hERG K(+) channels with a particular focus on nuclear magnetic resonance studies of the domains of the hERG K(+) channel.
[NMR paper] An NMR investigation of the structure, function and role of the hERG channel selectivity filter in the long QT syndrome.
An NMR investigation of the structure, function and role of the hERG channel selectivity filter in the long QT syndrome.
Related Articles An NMR investigation of the structure, function and role of the hERG channel selectivity filter in the long QT syndrome.
Biochim Biophys Acta. 2013 Mar 5;
Authors: Gravel AE, Arnold AA, Dufourc EJ, Marcotte I
Abstract
The human ether-a-go-go-related gene (hERG) voltage-gated K+ channels are located in heart cell membranes and hold a unique selectivity filter (SF) amino acid sequence (SVGFG) as compared...
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03-12-2013 07:09 PM
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
Proteins. 2011 May 16;
Authors: Gayen S, Li Q, Chen AS, Nguyen TH, Huang Q, Hill J, Kang C
The human Ether-à-go-go Related Gene (hERG) potassium channel plays an important role in the heart by controlling the rapid delayed rectifier current. The N-terminal 135 residues (NTD) contain a Per-Arnt-Sim (PAS) domain and an N-terminal amphipathic helix....
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06-12-2011 12:15 AM
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Methods Enzymol. 2011;493:21-60
Authors: Acton TB, Xiao R, Anderson S, Aramini J, Buchwald WA, Ciccosanti C, Conover K, Everett J, Hamilton K, Huang YJ, Janjua H, Kornhaber G, Lau J, Lee DY, Liu G, Maglaqui M, Ma L, Mao L, Patel D, Rossi P, Sahdev S, Shastry R, Swapna GV, Tang Y, Tong S, Wang D, Wang H, Zhao L, Montelione GT
In this chapter, we...
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03-05-2011 01:02 PM
[NMR paper] Thermodynamic insights into proteins from NMR spin relaxation studies.
Thermodynamic insights into proteins from NMR spin relaxation studies.
Related Articles Thermodynamic insights into proteins from NMR spin relaxation studies.
Curr Opin Struct Biol. 2001 Oct;11(5):555-9
Authors: Spyracopoulos L, Sykes BD
NMR spin relaxation measurements of picosecond to nanosecond timescale backbone and sidechain fluctuations of protein molecules, and subsequent entropic interpretation yield interesting, but sometimes counterintuitive, insights into proteins. The stabilities of proteins and protein interactions are achieved...
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11-19-2010 08:44 PM
[NMR paper] NMR studies on the structure/function correlations of T-cell-epitope analogs from per
NMR studies on the structure/function correlations of T-cell-epitope analogs from pertussis toxin.
Related Articles NMR studies on the structure/function correlations of T-cell-epitope analogs from pertussis toxin.
Eur J Biochem. 1998 Jun 1;254(2):313-7
Authors: Scarselli M, Esposito G, De Magistris MT, Domenighini M, Rappuoli R, Burroni G, Bernini A, Niccolai N
A synthetic tridecapeptide, corresponding to the 30-42 fragment of the S1 subunit of pertussis toxin, has been structurally characterised by using NMR spectroscopy. The molecule...
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11-17-2010 11:06 PM
NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
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11-09-2010 11:29 AM
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
Related Articles NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
J Biol Chem. 2010 Jul 28;
Authors: Montserret R, Saint N, Vanbelle C, Salvay AG, Simorre JP, Ebel C, Sapay N, Renisio JG, Bockmann A, Steinmann E, Pietschmann T, Dubuisson J, Chipot C, Penin F
The small membrane protein p7 of hepatitis C virus forms oligomers and exhibits ion channel activity essential for virus infectivity. These viroporin features render p7 an...
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08-17-2010 03:36 AM
NMR STUDIES OF STRUCTURE AND FUNCTION OF BIOLOGICAL MACROMOLECULES - Kurt Wüthrich
NMR STUDIES OF STRUCTURE AND FUNCTION OF BIOLOGICAL MACROMOLECULES - A Lecture by Kurt Wüthrich for The Nobel Foundation, 2002
http://nobelprize.org/nobel_prizes/chemistry/laureates/2002/wutrich-lecture.pdf
A video of the lecture can be found here:
http://nobelprize.org/nobel_prizes/chemistry/laureates/2002/wuthrich-lecture.html
Insights into hERG K+ channel structure and function from NMR studies.
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