CSF1 genomic organization biosynthesis and structure

The genomic organization and biosynthesis of the various forms of CSF-1 are summarized in Figure 2. Only the N-terminal 150 amino acids of the full-length 522 (human) or 520 (mouse) amino acid CSF-1 precursor are required for in vitro biological activity. The crystal structure of this region reveals that the CSF-1 monomer has an antiparallel four a-helical bundle/antiparallel (3 ribbon structure, similar to the structure of other cytokines, e.g. GM-CSF. The CSF-1 dimer is formed by disulfide bonding two monomers end-to-end, yielding a very flat, elongated structure.

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