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-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 language | English (US) |
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Pages (from-to) | 277-282 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 395 |
Issue number | 2-3 |
DOIs | |
State | Published - Oct 21 1996 |
Externally published | Yes |
Keywords
- Monocyte chemotactic protein
- Monomer-dimer
- NMR
- Solution structure
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology