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Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein‐3
Author(s) -
Kim Key-Sun,
Rajarathnam Krishnakumar,
Clark-Lewis Ian,
Sykes Brian D
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01024-1
Subject(s) - monomer , chemokine , chemistry , dimer , monocyte , chemotaxis , sedimentation equilibrium , in vivo , nuclear magnetic resonance spectroscopy , ultracentrifuge , biophysics , biochemistry , stereochemistry , biology , polymer , immunology , organic chemistry , receptor , microbiology and biotechnology
1 H‐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‐2 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.