Differences in Sulfotyrosine Binding amongst CXCR1 and CXCR2 Chemokine Ligands.

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 CX

SUBMITTER: Moussouras NA 

PROVIDER: S-EPMC5618543 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature