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

Abstract
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‐2 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.

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