?-Arrestins (?arrs) are functionally versatile proteins that play critical roles in the G-protein-coupled receptor (GPCR) signaling pathways. While it is well established that the phosphorylated receptor tail plays a central role in ?arr activation, emerging evidence highlights the contribution from membrane lipids. However, detailed molecular mechanisms of ?arr activation by different binding partners remain elusive. In this work, we present a comprehensive study of the structural changes in...
[ASAP] Unveiling the Surface Structure of ZnO Nanorods and H2 Activation Mechanisms with 17O NMR Spectroscopy
Unveiling the Surface Structure of ZnO Nanorods and H2 Activation Mechanisms with 17O NMR Spectroscopy
Benteng Song, Yuhong Li, Xin-Ping Wu, Fang Wang, Ming Lin, Yunhua Sun, Ai-ping Jia, Xiang Ning, Li Jin, Xiaokang Ke, Zhiwu Yu, Gang Yang, Wenhua Hou, Weiping Ding, Xue-Qing Gong, and Luming Peng?
https://pubs.acs.org/cms/10.1021/jacs.2c08356/asset/images/medium/ja2c08356_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.2c08356
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12-19-2022 01:33 AM
[NMR paper] Biphasic activation of beta-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR
Biphasic activation of beta-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR
?-arrestins (?arrs) play multifaceted roles in the function of G protein-coupled receptors (GPCRs). ?arrs typically interact with phosphorylated C-terminal tail (C tail) and transmembrane core (TM core) of GPCRs. However, the effects of the C tail- and TM core-mediated interactions on the conformational activation of ?arrs have remained elusive. Here, we show the conformational changes for ?arr activation upon the C tail- and TM core-mediated interactions with a prototypical GPCR by nuclear......
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12-10-2021 07:19 PM
[NMR paper] Phosphorylation-induced conformation of ?2-adrenoceptor related to arrestin recruitment revealed by NMR.
Phosphorylation-induced conformation of ?2-adrenoceptor related to arrestin recruitment revealed by NMR.
Related Articles Phosphorylation-induced conformation of ?2-adrenoceptor related to arrestin recruitment revealed by NMR.
Nat Commun. 2018 Jan 15;9(1):194
Authors: Shiraishi Y, Natsume M, Kofuku Y, Imai S, Nakata K, Mizukoshi T, Ueda T, Iwaï H, Shimada I
Abstract
The C-terminal region of G-protein-coupled receptors (GPCRs), stimulated by agonist binding, is phosphorylated by GPCR kinases, and the phosphorylated GPCRs bind to...
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01-18-2018 12:41 PM
Protein Plaques in Huntington's Patients Have Distinct Structures That Hint at Disease Mechanisms - Huntington's Disease News
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Protein Plaques in Huntington's Patients Have Distinct Structures That Hint at Disease Mechanisms
Huntington's Disease News
Researchers at the University of Pittsburgh School of Medicine used advanced nuclear magnetic resonance spectroscopy to directly assess and characterize huntingtin fibrils and other polyglutamine aggregates. Results showed that, unlike what previous ...
Protein Plaques in Huntington's Patients Have Distinct Structures That Hint at Disease Mechanisms - Huntington's Disease News
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02-06-2016 03:05 AM
[NMR paper] Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Nat Commun. 2015;6:8202
Authors: Yang F, Yu X, Liu C, Qu CX, Gong Z, Liu HD, Li FH, Wang HM, He DF, Yi F, Song C, Tian CL, Xiao KH, Wang JY, Sun JP
Abstract
Specific arrestin conformations are coupled to distinct downstream effectors, which underlie the functions of many...
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09-09-2015 11:49 AM
[NMR paper] Mechanisms of amyloid formation revealed by solution NMR.
Mechanisms of amyloid formation revealed by solution NMR.
Related Articles Mechanisms of amyloid formation revealed by solution NMR.
Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:86-104
Authors: Karamanos TK, Kalverda AP, Thompson GS, Radford SE
Abstract
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details...
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08-19-2015 03:24 PM
Mechanisms of amyloid formation revealed by solution NMR
Mechanisms of amyloid formation revealed by solution NMR
Publication date: Available online 26 May 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Theodoros K. Karamanos , Arnout P. Kalverda , Gary S. Thompson , Sheena E. Radford</br>
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details about the mechanism of...
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05-28-2015 12:56 AM
[NMR paper] Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Nucleic Acids Res. 2013 Aug 27;
Authors: Barabás O, Németh V, Bodor A, Perczel A, Rosta E, Kele Z, Zagyva I, Szabadka Z, Grolmusz VI, Wilmanns M, Vértessy BG
Abstract
Enzymatic synthesis...
Distinct activation mechanisms of ?-arrestin-1 revealed by 19F NMR spectroscopy
Linear Mode
