Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy [Biophysics and Computational Biology]
Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy [Biophysics and Computational Biology]
Ethanol consumption leads to a wide range of pharmacological effects by acting on the signaling proteins in the human nervous system, such as ion channels. Despite its familiarity and biological importance, very little is known about the molecular mechanisms underlying the ethanol action, due to extremely weak binding affinity and... Read More
PNAS:
Number: 15
Volume: 115
Did you find this post helpful? |
Similar Threads
Thread
Thread Starter
Forum
Replies
Last Post
[NMR paper] Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.
Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.
Related Articles Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2018 Mar 26;:
Authors: Toyama Y, Kano H, Mase Y, Yokogawa M, Osawa M, Shimada I
Abstract
Ethanol consumption leads to a wide range of pharmacological effects by acting on the signaling proteins in the human nervous system,...
nmrlearner
Journal club
0
03-28-2018 02:16 PM
Fluorine-19 NMR and computational quantification of isoflurane binding to the voltage-gated sodium channel NaChBac [Biophysics and Computational Biology]
Fluorine-19 NMR and computational quantification of isoflurane binding to the voltage-gated sodium channel NaChBac
Monica N. Kinde, Vasyl Bondarenko, Daniele Granata, Weiming Bu, Kimberly C. Grasty, Patrick J. Loll, Vincenzo Carnevale, Michael L. Klein, Roderic G. Eckenhoff, Pei Tang, Yan Xu...
Date: 2016-11-29
Voltage-gated sodium channels (NaV) play an important role in general anesthesia. Electrophysiology measurements suggest that volatile anesthetics such as isoflurane inhibit NaV by stabilizing the inactivated state or altering the inactivation kinetics. Recent computational...
nmrlearner
Journal club
0
11-29-2016 09:02 PM
HIV-1 leader RNA dimeric interface revealed by NMR [Biophysics and Computational Biology]
HIV-1 leader RNA dimeric interface revealed by NMR
Laura R. Ganser, Hashim M. Al-Hashimi...
Date: 2016-11-22
The genomes of retroviruses, such as HIV, consist of two single-stranded RNAs held together as a dimer through noncovalent interactions near the 5?-end. Why retroviruses carry two copies of their genetic material when most other viruses carry a single copy is something of a mystery. The single-stranded genomic RNA (gRNA)... Read More
PNAS:
Number: 47
nmrlearner
Journal club
0
11-22-2016 08:26 PM
[NMR paper] Insights into the molecular basis of action of the AT1 antagonist losartan using a combined NMR spectroscopy and computational approach.
Insights into the molecular basis of action of the AT1 antagonist losartan using a combined NMR spectroscopy and computational approach.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Insights into the molecular basis of action of the AT1 antagonist losartan using a combined NMR spectroscopy and computational approach.
Biochim Biophys Acta. 2014 Mar;1838(3):1031-46
Authors: Zervou M, Cournia Z, Potamitis C, Patargias G, Durdagi S, Grdadolnik SG, Mavromoustakos T
...
nmrlearner
Journal club
0
03-26-2014 12:44 PM
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR [Biophysics and Computational Biology]
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
Kato, H., van Ingen, H., Zhou, B.-R., Feng, H., Bustin, M., Kay, L. E., Bai, Y....
Date: 2011-07-26
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility group nucleosomal (HMGN) protein family that regulates various chromatin functions, including transcription. Here, we report the architecture of the HMGN2-nucleosome...
nmrlearner
Journal club
0
07-26-2011 11:22 PM
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion [Biophysics and Computational Biology]
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion
Meinhold, D. W., Wright, P. E....
Date: 2011-05-31
Detailed understanding of protein function and malfunction hinges on the ability to characterize transiently populated states and the transitions between them. Here, we use 15N, , and 13CO NMR R2 relaxation dispersion to investigate spontaneous unfolding and refolding events of native apomyoglobin. Above pH 5.0, dispersion is dominated by processes involving fluctuations of the F-helix region, which...
nmrlearner
Journal club
0
05-31-2011 11:41 PM
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method [Biophysics and Computational Biology]
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
Verardi, R., Shi, L., Traaseth, N. J., Walsh, N., Veglia, G....
Date: 2011-05-31
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca2+-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and...
nmrlearner
Journal club
0
05-31-2011 11:41 PM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy [Biophysics and Computational Biology]
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
Masterson, L. R., Shi, L., Metcalfe, E., Gao, J., Taylor, S. S., Veglia, G....
Date: 2011-04-26
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these...