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MONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTUREMONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTURE
Structural highlights
FunctionCCL7_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 PubMed1H-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. See AlsoReferences |
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