Low-resolution structure of recombinant human granulocyte-macrophage colony stimulating factor.
A recombinant form of human granulocyte-macrophage colony stimulating factor (GM-CSF) which contains no carbohydrate has been crystallized. Multiple isomorphous replacement analysis using five heavy-atom derivatives has yielded an image of the structure at 6 A resolution that showed two molecules per asymmetric unit and allowed determination of the non-crystallographic symmetry transformation. The 6 A resolution result shows that the core of GM-CSF consists of four helices. The angles at which the helices pack together distinguishes this structure from known antiparallel four-helix bundle proteins. Consideration of the amino acid sequence properties and previous structural characterizations of GM-CSF leads to an assignment of the probable protein segments that form the helices.
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.
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Diederichs
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Jacques
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Boone
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Karplus
D016178:Granulocyte-Macrophage Colony-Stimulating Factor / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D016178:Granulocyte-Macrophage Colony-Stimulating Factor