1RHG
THE STRUCTURE OF GRANULOCYTE-COLONY-STIMULATING FACTOR AND ITS RELATIONSHIP TO THOSE OF OTHER GROWTH FACTORS
Summary for 1RHG
| Entry DOI | 10.2210/pdb1rhg/pdb |
| Descriptor | GRANULOCYTE COLONY-STIMULATING FACTOR (2 entities in total) |
| Functional Keywords | growth factor |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P09919 |
| Total number of polymer chains | 3 |
| Total formula weight | 56056.69 |
| Authors | Hill, C.P.,Osslund, T.D.,Eisenberg, D. (deposition date: 1993-01-29, release date: 1994-01-31, Last modification date: 2024-10-30) |
| Primary citation | Hill, C.P.,Osslund, T.D.,Eisenberg, D. The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc.Natl.Acad.Sci.USA, 90:5167-5171, 1993 Cited by PubMed Abstract: We have determined the three-dimensional structure of recombinant human granulocyte-colony-stimulating factor by x-ray crystallography. Phases were initially obtained at 3.0-A resolution by multiple isomorphous replacement and were refined by solvent flattening and by averaging of the electron density of the three molecules in the asymmetric unit. The current R factor is 21.5% for all data between 6.0- and 2.2-A resolution. The structure is predominantly helical, with 104 of the 175 residues forming a four-alpha-helix bundle. The only other secondary structure is also helical. In the loop between the first two long helices a four-residue 3(10)-helix is immediately followed by a 6-residue alpha-helix. Three residues in the short connection between the second and third bundle helices form almost one turn of left-handed helix. The up-up-down-down connectivity with two long crossover connections has been reported previously for five other proteins, which like granulocyte-colony-stimulating factor are all signaling ligands: growth hormone, granulocyte/macrophage-colony-stimulating factor, interferon beta, interleukin 2, and interleukin 4. Structural similarity among these growth factors occurs despite the absence of similarity in their amino acid sequences. Conservation of this tertiary structure suggests that these different growth factors might all bind to their respective sequence-related receptors in an equivalent manner. PubMed: 7685117DOI: 10.1073/pnas.90.11.5167 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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