ArticleInternational journal of molecular sciences2017
Differences in Sulfotyrosine Binding amongst CXCR1 and CXCR2 Chemokine Ligands.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Selection Pressure Regulates the Evolution-Structure-Function Paradigm of Monocyte Chemoattractant Protein Family.Journal of molecular evolution · 2025Article
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- The TRIM33 Bromodomain Recognizes Histone Lysine Lactylation.ACS chemical biology · 2024Article
- Sulfoproteomics Workflow with Precursor Ion Accurate Mass Shift Analysis Reveals Novel Tyrosine Sulfoproteins in the Golgi.Journal of proteome research · 2024Article
- Article
- Enhanced tyrosine sulfation is associated with chronic kidney disease-related atherosclerosis.BMC biology · 2023Article
- Fragment-based drug discovery of small molecule ligands for the human chemokine CCL28.SLAS discovery : advancing life sciences R & D · 2023Article
- TPST2-mediated receptor tyrosine sulfation enhances leukocidin cytotoxicity andFrontiers in immunology · 2023Article
- Multifaceted Roles of Chemokine C-X-C Motif Ligand 7 in Inflammatory Diseases and Cancer.Frontiers in pharmacology · 2022Review
- Structural Features of an Extended C-Terminal Tail Modulate the Function of the Chemokine CCL21.Biochemistry · 2020Article
- Host-Receptor Post-Translational Modifications Refine Staphylococcal Leukocidin Cytotoxicity.Toxins · 2020Article
- Insights on CXC chemokine receptor 2 in breast cancer: An emerging target for oncotherapy.Oncology letters · 2019Review
- Regulation of Chemokine-Receptor Interactions and Functions.International journal of molecular sciences · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Tyrosine sulfation, a post-translational modification found on many chemokine receptors, typically increases receptor affinity for the chemokine ligand. A previous bioinformatics analysis suggested that a sulfotyrosine (sY)-binding site on the surface of the chemokine CXCL12 may be conserved throughout the chemokine family. However, the extent to which receptor tyrosine sulfation contributes to chemokine binding has been examined in only a few instances. Computational solvent mapping correctly identified the conserved sulfotyrosine-binding sites on CXCL12 and CCL21 detected by nuclear magnetic resonance (NMR) spectroscopy, demonstrating its utility for hot spot analysis in the chemokine family. In this study, we analyzed five chemokines that bind to CXCR2, a subset of which also bind to CXCR1, to identify hot spots that could participate in receptor binding. A cleft containing the predicted sulfotyrosine-binding pocket was identified as a principal hot spot for ligand binding on the structures of CXCL1, CXCL2, CXCL7, and CXCL8, but not CXCL5. Sulfotyrosine titrations monitored via NMR spectroscopy showed specific binding to CXCL8, but not to CXCL5, which is consistent with the predictions from the computational solvent mapping. The lack of CXCL5-sulfotyrosine interaction and the presence of CXCL8-sulfotyrosine binding suggests a role for receptor post-translational modifications regulating ligand selectivity.
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Registered trials
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