PDBsum entry: 1rhg

Growth factor

PDB id: 1rhg

Contents

Protein chains

145 a.a. *

144 a.a. *

Waters ×120

* Residue conservation analysis

PDB id:

1rhg

Name:

Growth factor

Title:

The structure of granulocyte-colony-stimulating factor and its relationship to those of other growth factors

Structure:

Granulocyte colony-stimulating factor. Chain: a, b, c. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

Biol. unit:

Trimer (from PQS)

Resolution:

2.20Å R-factor: 0.215

Authors:

C.P.Hill,T.D.Osslund,D.Eisenberg

Key ref:

C.P.Hill et al. (1993). The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc Natl Acad Sci U S A, 90, 5167-5171. PubMed id: 7685117 DOI: 10.1073/pnas.90.11.5167

Date:

29-Jan-93 Release date: 31-Jan-94

Protein chains

P09919  (CSF3_HUMAN) -  Granulocyte colony-stimulating factor

Seq: 207 a.a.

Struc: 145 a.a.

Protein chain

P09919  (CSF3_HUMAN) -  Granulocyte colony-stimulating factor

Seq: 207 a.a.

Struc: 144 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (2 terms)
• Biological process: immune response (5 terms)
• Biochemical function: enzyme binding (4 terms)

DOI no: 10.1073/pnas.90.11.5167

Proc Natl Acad Sci U S A 90:5167-5171 (1993)

PubMed id: 7685117

The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors.

C.P.Hill, T.D.Osslund, D.Eisenberg.

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.