Kim, Key-Sun Rajarathnam, K. Clark-Lewis, I. Sykes, B.D. 2024-01-21T20:14:47Z 2024-01-21T20:14:47Z 2021-09-02 1996-01 0014-5793 https://pubs.kist.re.kr/handle/201004/144877 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. English Elsevier B.V. Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein-3 Article 10.1016/0014-5793(96)01024-1 1 FEBS Letters, v.395, no.2-3, pp.277 - 282 FEBS Letters 395 2-3 277 282 N scopus 2-s2.0-0030597050 Article monocyte chemotactic protein 1 monocyte chemotactic protein 2 monocyte chemotactic protein 3 article dimerization in vitro study molecular weight nuclear magnetic resonance spectroscopy priority journal proprioception protein structure ultracentrifugation Monocyte chemotactic protein Monomer-dimer NMR Solution structure