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Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor
1Structural Biology Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720.
Science (New York, N.Y.)
|November 20, 1992
Summary
Macrophage colony-stimulating factor (M-CSF) dimer structure reveals insights into monocyte-macrophage development. Its structural similarity to other cytokines suggests conserved receptor binding mechanisms.
Area of Science:
- Cell Biology
- Structural Biology
- Immunology
Background:
- Macrophage colony-stimulating factor (M-CSF) is crucial for monocyte-macrophage lineage development and function.
- The active M-CSF form is a disulfide-linked dimer that activates its receptor's tyrosine kinase activity via dimerization.
Purpose of the Study:
- To determine the high-resolution structure of a recombinant human M-CSF dimer.
- To compare the structure of M-CSF with related cytokines and their receptors.
Main Methods:
- X-ray crystallography was used to determine the structure of the M-CSF dimer at 2.5 angstrom resolution.
Main Results:
- The M-CSF dimer structure consists of two four-alpha-helix bundles joined by an interchain disulfide bond.
- M-CSF monomers share structural similarities with granulocyte-macrophage colony-stimulating factor and human growth hormone.
- Unlike M-CSF, these other cytokines are monomeric and their receptors lack intrinsic tyrosine kinase activity.
Conclusions:
- The determined M-CSF dimer structure provides a molecular basis for its biological activity.
- Structural similarities suggest potential conservation in receptor binding determinants across M-CSF, GM-CSF, and growth hormone.
