Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein-3

Kim Key-Sun, Krishnakumar Rajarathnam, Ian Clark-Lewis, Brian D. Sykes

Research output: Contribution to journalArticlepeer-review

73 Scopus citations


1H-NMR spectroscopy and analytical ultracentrifugation studies reveal that monocyte chemoattractant protein-3 (MCP-3) is a monomer. NMR solution structure shows that MCP-3 adopts an α/β fold similar to what is observed in structures of other known chemokines. However, MCP-3 is unique in that it does not show a propensity to form dimers. The closely related chemokines MCP-1 and MCP-3 show a monomer-dimer equilibrium in sedimentation equilibrium studies (~ 0.2-2 mg/ml). As these proteins are present at nanomolar concentrations in vivo, the results suggest that they are monomeric at functional concentrations and that the monomer is the functionally significant form of MCP-1, MCP-2 and MCP-3.

Original languageEnglish (US)
Pages (from-to)277-282
Number of pages6
JournalFEBS Letters
Issue number2-3
StatePublished - Oct 21 1996
Externally publishedYes


  • Monocyte chemotactic protein
  • Monomer-dimer
  • NMR
  • Solution structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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