Related ArticlesNMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates.
J Biol Chem. 2016 Nov 18;:
Authors: Poms M, Ansorge P, Martinez-Gil L, Jurt S, Gottstein D, Fracchiolla KE, Cohen LS, Guentert P, Mingarro I, Naider F, Zerbe O
Abstract
Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot et al., Biochemistry 29(1990), 4031) is postulated to proceed in 2 steps: Partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significantly stabilized upon interaction with TM2, forming a helical hairpin reported previously (Neumoin et al., Biophys. J. 96(2009), 3187), and in this case the protein integrates into the hydrophobic interior of the micelle. TM123 displays a strong tendency to oligomerize, but hydrogen exchange data reveal that the center of TM3 is solvent exposed. In all GPCRs so-far structurally characterized TM7 forms many contacts with TM1 and TM2. In our study TM127 integrates well into the hydrophobic environment, but TM7 does not stably pack against the remaining helices. Topology mapping in microsomal membranes also indicates that TM1 does not integrate in a membrane-spanning fashion, but that TM12, TM123 and TM127 adopt predominantly native-like topologies. The data from our study would be consistent with the retention of individual helices of incompletely synthesized GPCRs in the vicinity of the translocon until the complete receptor is released into the membrane interior.
PMID: 27864365 [PubMed - as supplied by publisher]
Investigation of the Binding Interaction of FattyAcids with Human G Protein-Coupled Receptor 40 Using a Site-SpecificFluorescence Probe by Flow Cytometry
Investigation of the Binding Interaction of FattyAcids with Human G Protein-Coupled Receptor 40 Using a Site-SpecificFluorescence Probe by Flow Cytometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00079/20160317/images/medium/bi-2016-00079r_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00079
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/OkklAJsEsGE
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03-18-2016 04:29 AM
NMR as a tool to identify and characterize protein folding intermediates
NMR as a tool to identify and characterize protein folding intermediates
Available online 12 September 2012
Publication year: 2012
Source:Archives of Biochemistry and Biophysics</br>
</br>
NMR spectroscopy is one of the few biophysical methods that can provide atomic-level insight into the conformation of partially folded states and/or intermediates present along the protein folding pathway. Such studies are important not only within the context of the protein folding problem, but also to push forward the technique, due to the challenging nature of the systems studied....
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02-03-2013 10:13 AM
The Chemoselective Reactions of Tyrosine-Containing G-Protein-Coupled Receptor Peptides with [Cp*Rh(H2O)3](OTf)2, Including 2D NMR Structures and the Biological Consequences
The Chemoselective Reactions of Tyrosine-Containing G-Protein-Coupled Receptor Peptides with (OTf)2, Including 2D NMR Structures and the Biological Consequences
H. Bauke Albada, Florian Wieberneit, Ingrid Dijkgraaf, Jessica H. Harvey, Jennifer L. Whistler, Raphael Stoll, Nils Metzler-Nolte and Richard H. Fish
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303010k/aop/images/medium/ja-2012-03010k_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303010k
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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06-16-2012 06:01 AM
[NMR paper] Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled r
Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
Related Articles Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
J Am Chem Soc. 2005 Jun 8;127(22):8010-1
Authors: Tian C, Breyer RM, Kim HJ, Karra MD, Friedman DB, Karpay A, Sanders CR
The seven-transmembrane-spanning G protein-coupled receptor (GPCR) superfamily plays many important roles in basic biology, human health, and human disease. Here, well-resolved solution NMR spectra are presented for a human...
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11-25-2010 08:21 PM
[NMR paper] Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solutio
Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Related Articles Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3409-13
Authors: Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the...
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11-24-2010 09:25 PM
[NMR paper] The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor
The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
Related Articles The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
Biopolymers. 2003 Jun;69(2):201-15
Authors: Miskolzie M, Kotovych G
The tertiary structure of the pain modulating and anti-opiate neuropeptide, human neuropeptide AF (NPAF) (the sequence is AGEGLNSQFWSLAAPQRF-NH(2)), was determined by (1)H-NMR. The structure of NPAF was determined in two solvent systems, namely 50%/50%...
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11-24-2010 09:01 PM
[NMR paper] Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Sac
Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
Related Articles Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
Biopolymers. 1998 Nov;46(6):343-57
Authors: Arshava B, Liu SF, Jiang H, Breslav M, Becker JM, Naider F
Peptides representing both loop and the sixth transmembrane regions of the alpha-factor receptor of Saccharomyces cerevisiae were synthesized by...
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11-17-2010 11:15 PM
[NMR paper] Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide ex
Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopy.
Related Articles Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopy.
Biochemistry. 1993 Jun 22;32(24):6152-6
Authors: Mullins LS, Pace CN, Raushel FM
The rate of hydrogen bond formation at individual amino acid residues in ribonuclease T1 (RNase T1) has been investigated by the hydrogen-deuterium exchange-2D NMR (HDEx-2D NMR) technique (Udgaonkar...