ArticleProtein science : a publication of the Protein Society2014
The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
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- 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
- Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study.Molecules (Basel, Switzerland) · 2018Article
- CPP-E1A fusion peptides inhibit CtBP-mediated transcriptional repression.Molecular oncology · 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
- Regulation of Chemokine Function: The Roles of GAG-Binding and Post-Translational Nitration.International journal of molecular sciences · 2017Review
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- Peptides derived from CXCL8 based on in silico analysis inhibit CXCL8 interactions with its receptor CXCR1.Scientific reports · 2015Article
- Inherent dynamics within the Crimean-Congo Hemorrhagic fever virus protease are localized to the same region as substrate interactions.Protein science : a publication of the Protein Society · 2015Article
- Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.Protein science : a publication of the Protein Society · 2015Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Interleukin-8 (CXCL8, IL-8) is a proinflammatory chemokine important for the regulation of inflammatory and immune responses via its interaction with G-protein coupled receptors, including CXC receptor 1 (CXCR1). CXCL8 exists as both a monomer and as a dimer at physiological concentrations, yet the molecular basis of CXCL8 interaction with its receptor as well as the importance of CXCL8 dimer formation remain poorly characterized. Although several biological studies have indicated that both the CXCL8 monomer and dimer are active, biophysical studies have reported conflicting results regarding the binding of CXCL8 to CXCR1. To clarify this problem, we expressed and purified a peptide (hCXCR1pep) corresponding to the N-terminal region of human CXCR1 (hCXCR1) and utilized nuclear magnetic resonance (NMR) spectroscopy to interrogate the binding of wild-type CXCL8 and a previously reported mutant (CXCL8M) that stabilizes the monomeric form. Our data reveal that the CXCL8 monomer engages hCXCR1pep with a slightly higher affinity than the CXCL8 dimer, but that the CXCL8 dimer does not dissociate upon binding hCXCR1pep. These investigations also showed that CXCL8 is dynamic on multiple timescales, which may help explain the versatility in this interleukin for engaging its target receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.