ArticleBiochemistry2011
Local and global dynamics of the G protein-coupled receptor CXCR1.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed.
- Article
- The Dynamics of the Neuropeptide Y Receptor Type 1 Investigated by Solid-State NMR and Molecular Dynamics Simulation.Molecules (Basel, Switzerland) · 2020Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.Angewandte Chemie (International ed. in English) · 2020Article
- Integration of Cell-Free Expression and Solid-State NMR to Investigate the Dynamic Properties of Different Sites of the Growth Hormone Secretagogue Receptor.Frontiers in pharmacology · 2020Article
- Extramembranous Regions in G Protein-Coupled Receptors: Cinderella in Receptor Biology?The Journal of membrane biology · 2019Review
- Solution NMR spectroscopy of GPCRs: Residue-specific labeling strategies with a focus onMethods in cell biology · 2019Article
- Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study.Molecules (Basel, Switzerland) · 2018Article
- Interaction of Monomeric Interleukin-8 with CXCR1 Mapped by Proton-Detected Fast MAS Solid-State NMR.Biophysical journal · 2017Article
- Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.Journal of biomolecular NMR · 2017Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.Scientific reports · 2017Article
- Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).Journal of biomolecular NMR · 2015Article
- The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.Journal of biomolecular NMR · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.Protein science : a publication of the Protein Society · 2015Article
- Multiple acquisition/multiple observation separated local field/chemical shift correlation solid-state magic angle spinning NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Dynamic conformational switching in the chemokine ligand is essential for G-protein-coupled receptor activation.The Biochemical journal · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The local and global dynamics of the chemokine receptor CXCR1 are characterized using a combination of solution NMR and solid-state NMR experiments. In isotropic bicelles (q = 0.1), only 13% of the expected number of backbone amide resonances is observed in (1)H/(15)N HSQC solution NMR spectra of uniformly (15)N-labeled samples; extensive deuteration and the use of TROSY made little difference in the 800 MHz spectra. The limited number of observed amide signals is ascribed to mobile backbone sites and assigned to specific residues in the protein; 19 of the signals are from residues at the N-terminus and 25 from residues at the C-terminus. The solution NMR spectra display no evidence of local backbone motions from residues in the transmembrane helices or interhelical loops of CXCR1. This finding is reinforced by comparisons of solid-state NMR spectra of both magnetically aligned and unoriented bilayers containing either full-length or doubly N- and C-terminal truncated CXCR1 constructs. CXCR1 undergoes rapid rotational diffusion about the normal of liquid crystalline phospholipid bilayers; reductions in the frequency span and a change to axial symmetry are observed for both carbonyl carbon and amide nitrogen chemical shift powder patterns of unoriented samples containing (13)C- and (15)N-labeled CXCR1. In contrast, when the phospholipids are in the gel phase, CXCR1 does not undergo rapid global reorientation on the 10(4) Hz time scale defined by the carbonyl carbon and amide nitrogen chemical shift powder patterns.
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