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

35 Citations (Scopus)

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

Fingerprint

Chemokine CXCL1
Glycosaminoglycans
Chemokines
Dimers
Heparin
Neutrophil Infiltration
Neutrophils
Structural integrity
Structural properties

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Molecular basis of glycosaminoglycan heparin binding to the chemokine CXCL1 dimer. / Poluri, Krishna Mohan; Joseph, Prem Raj B; Sawant, Kirti V.; Rajarathnam, Krishna.

In: Journal of Biological Chemistry, Vol. 288, No. 35, 30.08.2013, p. 25143-25153.

Research output: Contribution to journalArticle

Poluri, Krishna Mohan ; Joseph, Prem Raj B ; Sawant, Kirti V. ; Rajarathnam, Krishna. / Molecular basis of glycosaminoglycan heparin binding to the chemokine CXCL1 dimer. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 35. pp. 25143-25153.
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