Structure-activity relationships of chemokines

I. Clark-Lewis, K. S. Kim, K. Rajarathnam, J. H. Gong, B. Dewald, B. Moser, M. Baggiolini, B. D. Sykes

Research output: Contribution to journalArticlepeer-review

341 Scopus citations


Structural analysis of chemokines has revealed that the α/β structural-fold is highly conserved among both the CXC and CC chemokine classes, Although dimerization and aggregation is often observed, the chemokines function as monomers. The critical receptor binding regions are in the NH2-terminal 20 residues of the protein and are the least ordered in solution. The flexible NH2-terminal region is the most critical receptor binding site and a second site also exists in the loop that follows the two disulfides, The well ordered regions are not directly involved in receptor binding but, along with the disulfides, they provide a scaffold that determines the conformation of the sites that are critical for receptor binding. These general requirements for function are common to all the chemokines. For the CC chemokines, receptor activation and receptor binding regions are separate within the 10 residue NH2-terminal region, This has allowed identification of high affinity analogs that do not activate the receptor and are potent antagonists.

Original languageEnglish (US)
Pages (from-to)703-711
Number of pages9
JournalJournal of Leukocyte Biology
Issue number5
StatePublished - 1995
Externally publishedYes


  • Inflammation
  • Interleukin-8
  • Monocyte chemoattractant protein
  • Peptide synthesis
  • Protein engineering

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Cell Biology


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