Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3.
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Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD
Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3.
FEBS Lett. 1996 Oct 21;395(2-3):277-82.
- PubMed ID
- 8898111 [ View in PubMed]
- 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 alphabeta 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 (approximately 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.