[NMR paper] Illuminating GPCR signaling mechanisms by NMR spectroscopy with stable-isotope labeled receptors
Illuminating GPCR signaling mechanisms by NMR spectroscopy with stable-isotope labeled receptors
G protein-coupled receptors (GPCRs) exhibit remarkable structural plasticity, which underlies their capacity to recognize a wide range of extracellular molecules and interact with intracellular partner proteins. Nuclear magnetic resonance (NMR) spectroscopy is uniquely well-suited to investigate GPCR structural plasticity, enabled by stable-isotope "probes" incorporated into receptors that inform on structure and dynamics. Progress with stable-isotope labeling methods in Eukaryotic...
Structural investigation of glycan recognition by the ERAD quality control lectin Yos9
Structural investigation of glycan recognition by the ERAD quality control lectin Yos9
Abstract
Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoproteins that fail to attain their native conformation in the ER expose a distinct oligosaccharide structure, a terminal α1,6-linked mannose residue, that is specifically recognized by the mannose 6-phoshate...
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11-25-2018 06:02 AM
[NMR paper] Understanding GPCR Recognition and Folding from NMR Studies of Fragments.
Understanding GPCR Recognition and Folding from NMR Studies of Fragments.
Related Articles Understanding GPCR Recognition and Folding from NMR Studies of Fragments.
RSC Adv. 2018;8(18):9858-9870
Authors: Marino J, Walser R, Poms M, Zerbe O
Abstract
Cotranslational protein folding is a vectorial process, and for membrane proteins, N-terminal helical segments are the first that become available for membrane insertion. While structures of many G-protein coupled receptors (GPCRs) in various states have been determined, the details of...
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05-09-2018 02:49 AM
[NMR paper] Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state
Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.
Related Articles Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.
Biophys J. 2002 Feb;82(2):1017-29
Authors: Hatcher ME, Hu JG, Belenky M, Verdegem P, Lugtenburg J, Griffin RG, Herzfeld J
By varying the pH, the D85N mutant of bacteriorhodopsin provides models for several photocycle intermediates of the wild-type protein in which D85 is protonated. At pH 10.8, NMR spectra of...
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11-24-2010 08:49 PM
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machiner
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machineries
* In the context of a project funded by European Research Council, two postdoctoral positions are available at the Structural Biology Institute in Grenoble (France) to study by real-time NMR the Folding & Mechanisms of Protein Quality Control (PQC) Machineries. Selected candidates will use latest NMR technologies developed at IBS to characterize self-assembly and functionally important structural rearrangements of large PQC machineries isolated at IBS.
* The laboratory host…
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Anionic phospholipids control mechanisms of GPCR-G protein recognition - Nature.com
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