Molecular basis of glycosaminoglycan heparin binding to the chemokine CXCL1 dimer

Krishna Mohan Poluri, Prem Raj B. Joseph, Kirti V. Sawant, Krishna Rajarathnam

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

Background: Glycosaminoglycan (GAG)-chemokine dimer interactions regulate neutrophil trafficking, but the molecular basis underlying their interactions is not well understood. Results:NMRstudies of murine CXCL1 indicate that heparin spans the dimer interface and enhances its structural integrity and stability. Conclusion: Heparin binding modulates multiple structural properties of the chemokine dimer. Significance: This study provides novel structural insights into how chemokine dimers orchestrate neutrophil recruitment.

Original languageEnglish (US)
Pages (from-to)25143-25153
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number35
DOIs
StatePublished - Aug 30 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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