ArticleThe FEBS journal2018
The solution structure of monomeric CCL5 in complex with a doubly sulfated N-terminal segment of CCR5.
Article in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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
24 citing papers in PubMed, 42 citations in OpenAlex.
- Chemokine-Binding All-D-CLIPS Peptides Identified Using Mirror-Image Phage Display.ACS chemical biology · 2025Article
- Filamentous chemokine CCL5 structure and the functional aspects.Scientific reports · 2025Article
- The chemokine receptor CCR5: multi-faceted hook for HIV-1.Retrovirology · 2024Review
- NMR indicates the N-termini of PSGL1 and CCR7 bind competitively to the chemokine CCL21.Biochemistry and biophysics reports · 2023Article
- Naming the Barriers between Anti-CCR5 Therapy, Breast Cancer and Its Microenvironment.International journal of molecular sciences · 2022Review
- Structural Insights into Molecular Recognition by Human Chemokine CCL19.Biochemistry · 2022Article
- Filling the Gaps in Antagonist CCR5 Binding, a Retrospective and Perspective Analysis.Frontiers in immunology · 2022Article
- Computational study of the structural ensemble of CC chemokine receptor type 5 (CCR5) and its interactions with different ligands.PloS one · 2022Article
- The marriage of chemokines and galectins as functional heterodimers.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- The dimeric form of CXCL12 binds to atypical chemokine receptor 1.Science signaling · 2021Article
- Structural basis for chemokine recognition and receptor activation of chemokine receptor CCR5.Nature communications · 2021Article
- Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist.Science advances · 2021Article
- Article
- The methylJournal of biomolecular NMR · 2020Article
- A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020Review
- Comparative modeling and docking of chemokine-receptor interactions with Rosetta.Biochemical and biophysical research communications · 2020Article
- Semisynthesis of an evasin from tick saliva reveals a critical role of tyrosine sulfation for chemokine binding and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- N-terminal Backbone Pairing Shifts in CCL5-International journal of molecular sciences · 2020Article
- Structural basis of chemokine and receptor interactions: Key regulators of leukocyte recruitment in inflammatory responses.Protein science : a publication of the Protein Society · 2020Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
The inflammatory chemokine CCL5, which binds the chemokine receptor CCR5 in a two-step mechanism so as to activate signaling pathways in hematopoetic cells, plays an important role in immune surveillance, inflammation, and development as well as in several immune system pathologies. The recently published crystal structure of CCR5 bound to a high-affinity variant of CCL5 lacks the N-terminal segment of the receptor that is post-translationally sulfated and is known to be important for high-affinity binding. Here, we report the NMR solution structure of monomeric CCL5 bound to a synthetic doubly sulfated peptide corresponding to the missing first 27 residues of CCR5. Our structures show that two sulfated tyrosine residues, sY10 and sY14, as well as the unsulfated Y15 form a network of strong interactions with a groove on a surface of CCL5 that is formed from evolutionarily conserved basic and hydrophobic amino acids. We then use our NMR structures, in combination with available crystal data, to create an atomic model of full-length wild-type CCR5:CCL5. Our findings reveal the structural determinants involved in the recognition of CCL5 by the CCR5 N terminus. These findings, together with existing structural data, provide a complete structural framework with which to understand the specificity of receptor:chemokine interactions. DATABASE: Structural data are available in the PDB under the accession number 6FGP.
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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.