ArticleJournal of molecular biology2011
Interactions of interleukin-8 with the human chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 57 citations in OpenAlex.
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- Selection of a picomolar antibody that targets CXCR2-mediated neutrophil activation and alleviates EAE symptoms.Nature communications · 2021Article
- Conformational plasticity and dynamic interactions of the N-terminal domain of the chemokine receptor CXCR1.PLoS computational biology · 2021Article
- A highly efficient method for the production and purification of recombinant human CXCL8.PloS one · 2021Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Therapeutic Interventions into Innate Immune Diseases by Means of Aptamers.Pharmaceutics · 2020Review
- Differential Dynamics Underlying the Gln27Glu Population Variant of the βThe Journal of membrane biology · 2019Article
- Tick saliva protein Evasin-3 modulates chemotaxis by disrupting CXCL8 interactions with glycosaminoglycans and CXCR2.The Journal of biological chemistry · 2019Article
- Interleukin-37 monomer is the active form for reducing innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- 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
- Heparin-bound chemokine CXCL8 monomer and dimer are impaired for CXCR1 and CXCR2 activation: implications for gradients and neutrophil trafficking.Open biology · 2017Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- New paradigms in chemokine receptor signal transduction: Moving beyond the two-site model.Biochemical pharmacology · 2016Review
- Peptides derived from CXCL8 based on in silico analysis inhibit CXCL8 interactions with its receptor CXCR1.Scientific reports · 2015Article
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- 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
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
CXCR1 is a receptor for the chemokine interleukin-8 (IL-8), a mediator of immune and inflammatory responses. Strategically located in the cell membrane, CXCR1 binds to IL-8 with high affinity and subsequently transduces a signal across the membrane bilayer to a G-protein-activated second messenger system. Here, we describe NMR studies of the interactions between IL-8 and human CXCR1 in lipid environments. Functional full-length and truncated constructs of CXCR1 and full-length IL-8 were uniformly (15)N-labeled by expression in bacteria followed by purification and refolding. The residues responsible for interactions between IL-8 and the N-terminal domain of CXCR1 were identified by specific chemical shift perturbations of assigned resonances on both IL-8 and CXCR1. Solution NMR signals from IL-8 in q=0.1 isotropic bicelles disappeared completely when CXCR1 in lipid bilayers was added in a 1:1 molar ratio, indicating that binding to the receptor-containing bilayers immobilizes IL-8 (on the ~10(5) Hz timescale) and broadens the signals beyond detection. The same solution NMR signals from IL-8 were less affected by the addition of N-terminal truncated CXCR1 in lipid bilayers, demonstrating that the N-terminal domain of CXCR1 is mainly responsible for binding to IL-8. The interaction is tight enough to immobilize IL-8 along with the receptor in phospholipid bilayers and is specific enough to result in well-aligned samples in oriented sample solid-state NMR spectra. A combination of solution NMR and solid-state NMR studies of IL-8 in the presence of various constructs of CXCR1 enables us to propose a model for the multistep binding process.
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