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• W2795708515 abstract "The inflammatory chemokine CCL 5, which binds the chemokine receptor CCR 5 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 CCR 5 bound to a high‐affinity variant of CCL 5 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 CCL 5 bound to a synthetic doubly sulfated peptide corresponding to the missing first 27 residues of CCR 5. Our structures show that two sulfated tyrosine residues, sY 10 and sY 14, as well as the unsulfated Y15 form a network of strong interactions with a groove on a surface of CCL 5 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 CCR 5: CCL 5. Our findings reveal the structural determinants involved in the recognition of CCL 5 by the CCR 5 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" @default.
• W2795708515 created "2018-04-13" @default.
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• W2795708515 date "2018-04-20" @default.
• W2795708515 modified "2023-10-15" @default.
• W2795708515 title "The solution structure of monomeric <scp>CCL</scp>5 in complex with a doubly sulfated N‐terminal segment of <scp>CCR</scp>5" @default.
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• W2795708515 doi "https://doi.org/10.1111/febs.14460" @default.
• W2795708515 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6433596" @default.
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