The structure of GM-CSF has been determined by both partial amino acid sequence analysis and by deduction from the nucleotide sequence of cDNA clones. Mature murine and human GM-CSFs contain 124 and 127 amino acids, respectively. In each species the mature protein is preceded by a 17 amino acid leader sequence. Although murine and human GM-CSF are 54% identical at the amino acid level, there is no cross-species biological activity. Both murine and human GM-CSF contain two potential N-linked glycosylation sites and two internal disulfide bridges. Native GM-CSF is glycosylated to approximately 23 kDa. Bacterial-derived, nonglycosylated GM-CSF has high biological activity, indicating that the attached carbohydrate is not absolutely required for the molecule to be functional. GM-CSF has been demonstrated by X-ray crystallography to combine a two-stranded antiparallel )3 sheet with an open bundle of four a helices. This structure is similar to that of other hematopoietic cytokines.

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