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Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12. | LitMetric

AI Article Synopsis

  • - The study investigates how the chemokine SDF-1 and its receptor CXCR4 are involved in stem cell homing and breast cancer spread (metastasis).
  • - Researchers determined the structure of SDF-1 when bound to CXCR4, highlighting the importance of three specific sulfotyrosine residues for the interaction's effectiveness.
  • - The findings suggest that while dimeric SDF-1 can trigger calcium mobilization in cells, it does not promote movement towards SDF-1, indicating it functions as a partial agonist, which could inform future drug development targeting CXCR4.

Article Abstract

Stem cell homing and breast cancer metastasis are orchestrated by the chemokine stromal cell-derived factor 1 (SDF-1) and its receptor CXCR4. Here, we report the nuclear magnetic resonance structure of a constitutively dimeric SDF-1 in complex with a CXCR4 fragment that contains three sulfotyrosine residues important for a high-affinity ligand-receptor interaction. CXCR4 bridged the SDF-1 dimer interface so that sulfotyrosines sTyr7 and sTyr12 of CXCR4 occupied positively charged clefts on opposing chemokine subunits. Dimeric SDF-1 induced intracellular Ca2+ mobilization but had no chemotactic activity; instead, it prevented native SDF-1-induced chemotaxis, suggesting that it acted as a potent partial agonist. Our work elucidates the structural basis for sulfotyrosine recognition in the chemokine-receptor interaction and suggests a strategy for CXCR4-targeted drug development.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2692298PMC
http://dx.doi.org/10.1126/scisignal.1160755DOI Listing

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