In the human proteome, 826 G-protein-coupled receptors (GPCRs) interact with extracellular stimuli to initiate cascades of intracellular signaling. Determining conformational dynamics and intermolecular interactions are key to understand GPCR function as a basis for drug design. X-ray crystallography and cryo-electron microscopy (cryo-EM) contribute molecular architectures of GPCRs and GPCR-signaling complexes. NMR spectroscopy is complementary by providing information on the dynamics of GPCR...
[NMR paper] G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling
G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling
G protein-coupled receptors (GPCRs) are a large membrane protein family found in higher organisms, including the human body. GPCRs mediate cellular responses to diverse extracellular stimuli and thus control key physiological functions, which makes them important targets for drug design. Signaling by GPCRs is related to the structure and dynamics of these proteins, which are modulated by extrinsic ligands as well as by...
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05-15-2022 06:54 AM
[NMR paper] Structural Biology of Human GPCR Drugs and Endogenous Ligands - Insights from NMR Spectroscopy.
Structural Biology of Human GPCR Drugs and Endogenous Ligands - Insights from NMR Spectroscopy.
Structural Biology of Human GPCR Drugs and Endogenous Ligands - Insights from NMR Spectroscopy.
Methods. 2020 Sep 07;:
Authors: Ferré G, Eddy M
Abstract
G protein-coupled receptors (GPCRs) represent the largest class of "druggable" proteins in the human genome. For more than a decade, crystal structures and, more recently, cryoEM structures of GPCR complexes have provided unprecedented insight into GPCR drug binding and cell...
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09-13-2020 09:18 AM
[NMR paper] Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-? Variants and Structural Analysis by Solution NMR Spectroscopy.
Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-? Variants and Structural Analysis by Solution NMR Spectroscopy.
Related Articles Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-? Variants and Structural Analysis by Solution NMR Spectroscopy.
PLoS One. 2015;10(10):e0139710
Authors: Dammers C, Gremer L, Neudecker P, Demuth HU, Schwarten M, Willbold D
Abstract
Alzheimer's disease (AD) is the leading cause of dementia in the elderly and is...
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10-06-2015 10:39 PM
[NMR paper] Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy
Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Naoki Kimata , Philip J. Reeves , Steven O. Smith</br>
G protein-coupled receptors (GPCRs) span cell membranes with seven transmembrane helices and respond to a diverse array of extracellular signals. Crystal structures of GPCRs have provided key insights into the architecture of these receptors and the role of conserved residues. However, the question of how ligand binding induces the...
[NMR paper] Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data.
Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data.
Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data.
Structure. 2014 Nov 6;22(12):1862-1874
Authors: Lemak A, Wu B, Yee A, Houliston S, Lee HW, Gutmanas A, Fang X, Garcia M, Semesi A, Wang YX, Prestegard JH, Arrowsmith CH
Abstract
Multidomain proteins in which individual domains are connected by linkers often possess inherent...
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12-03-2014 04:05 PM
Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data
Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data
Publication date: Available online 6 November 2014
Source:Structure</br>
Author(s): Alexander Lemak , Bin Wu , Adelinda Yee , Scott Houliston , Hsiau-Wei Lee , Aleksandras Gutmanas , Xianyang Fang , Maite Garcia , Anthony Semesi , Yun-Xing Wang , James*H. Prestegard , Cheryl*H. Arrowsmith</br>
Multidomain proteins in which individual domains are connected by linkers often possess inherent interdomain flexibility that significantly...
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11-07-2014 09:09 AM
[NMR paper] Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
J Biomol NMR. 2013 Aug 24;
Authors: Bernard D, Bédard M, Bilodeau J, Lavigne P
Abstract
Myc-interacting zinc finger protein-1 (Miz-1) is a BTB/POZ transcription factor that activates the...
GPCR structural characterization by NMR spectroscopy in solution
Linear Mode
