ArticleThe Journal of biological chemistry2016
Molecular Basis of Chemokine CXCL5-Glycosaminoglycan Interactions.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 54 citations in OpenAlex.
- CXCL5: A coachman to drive cancer progression.Frontiers in oncology · 2022Pooled it
- C-X-C Motif Chemokine Ligand 5 (CXCL5) Exhibits a U-Shaped Risk Profile for Mortality in Patients with Suspected Coronary Chest Pain.International journal of molecular sciences · 2026Article
- Structural Basis of Chemokine CXCL8 Monomer and Dimer Binding to Chondroitin Sulfate: Insights into Specificity and Plasticity.Biomolecules · 2026Article
- The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans.Nature communications · 2024Article
- Article
- Chemokine Cxcl1-Cxcl2 heterodimer is a potent neutrophil chemoattractant.Journal of leukocyte biology · 2023Article
- Article
- Solvent Model Benchmark for Molecular Dynamics of Glycosaminoglycans.Journal of chemical information and modeling · 2023Article
- NMR Methods for Characterization of Glycosaminoglycan-Chemokine Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Chemoenzymatic Synthesis of Heparan Sulfate Oligosaccharides having a Domain Structure.Angewandte Chemie (International ed. in English) · 2022Article
- Molecular dynamics simulations to understand glycosaminoglycan interactions in the free- and protein-bound states.Current opinion in structural biology · 2022Review
- Aqueous Molecular Dynamics for Understanding Glycosaminoglycan Recognition by Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- Combinatorial Virtual Library Screening Study of Transforming Growth Factor-β2-Chondroitin Sulfate System.International journal of molecular sciences · 2021Article
- Latest update on chemokine receptors as therapeutic targets.Biochemical Society transactions · 2021Review
- Neutrophil recruitment by chemokines Cxcl1/KC and Cxcl2/MIP2: Role of Cxcr2 activation and glycosaminoglycan interactions.Journal of leukocyte biology · 2021Article
- NMR Characterization of the Interactions Between Glycosaminoglycans and Proteins.Frontiers in molecular biosciences · 2021Review
- Rigorous analysis of free solution glycosaminoglycan dynamics using simple, new tools.Glycobiology · 2020Article
- Structural Insights Into How Proteoglycans Determine Chemokine-CXCR1/CXCR2 Interactions: Progress and Challenges.Frontiers in immunology · 2020Review
- Targeting Chemokine-Glycosaminoglycan Interactions to Inhibit Inflammation.Frontiers in immunology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Chemokines, a large family of highly versatile small soluble proteins, play crucial roles in defining innate and adaptive immune responses by regulating the trafficking of leukocytes, and also play a key role in various aspects of human physiology. Chemokines share the characteristic feature of reversibly existing as monomers and dimers, and their functional response is intimately coupled to interaction with glycosaminoglycans (GAGs). Currently, nothing is known regarding the structural basis or molecular mechanisms underlying CXCL5-GAG interactions. To address this missing knowledge, we characterized the interaction of a panel of heparin oligosaccharides to CXCL5 using solution NMR, isothermal titration calorimetry, and molecular dynamics simulations. NMR studies indicated that the dimer is the high-affinity GAG binding ligand and that lysine residues from the N-loop, 40s turn, β3 strand, and C-terminal helix mediate binding. Isothermal titration calorimetry indicated a stoichiometry of two oligosaccharides per CXCL5 dimer. NMR-based structural models reveal that these residues form a contiguous surface within a monomer and, interestingly, that the GAG-binding domain overlaps with the receptor-binding domain, indicating that a GAG-bound chemokine cannot activate the receptor. Molecular dynamics simulations indicate that the roles of the individual lysines are not equivalent and that helical lysines play a more prominent role in determining binding geometry and affinity. Further, binding interactions and GAG geometry in CXCL5 are novel and distinctly different compared with the related chemokines CXCL1 and CXCL8. We conclude that a finely tuned balance between the GAG-bound dimer and free soluble monomer regulates CXCL5-mediated receptor signaling and function.
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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.