Structural highlights
Function
[CCL7_HUMAN] Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3.,Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD FEBS Lett. 1996 Oct 21;395(2-3):277-82. PMID:8898111[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. PMID:8898111
