1BGE

CRYSTAL STRUCTURE OF CANINE AND BOVINE GRANULOCYTE-COLONY STIMULATING FACTOR (G-CSF)

Summary for 1BGE

• Entry DOI: 10.2210/pdb1bge/pdb
• Descriptor: GRANULOCYTE COLONY-STIMULATING FACTOR (2 entities in total)
• Functional Keywords: cytokine
• Biological source: Canis lupus familiaris (dog)
• Total number of polymer chains: 2
• Total formula weight: 37743.77

Authors

Lovejoy, B.,Cascio, D.,Eisenberg, D. (deposition date: 1993-04-27, release date: 1993-10-31, Last modification date: 2024-06-05)

Primary citation

Lovejoy, B.,Cascio, D.,Eisenberg, D.
Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF).
J.Mol.Biol., 234:640-653, 1993

PubMed Abstract: The crystal structures of recombinant canine and bovine granulocyte colony stimulating factor (G-CSF) have been determined by X-ray crystallography, using molecular replacement with recombinant human G-CSF as a model. G-CSF is a member of the cytokine family of glycoproteins that stimulate the differentiation and proliferation of blood cells. Human, bovine and canine G-CSF all have a molecular mass of about 19 kDa and share an amino acid sequence identity of about 80%. Two crystal forms of canine G-CSF have been solved. Form I recombinant canine G-CSF (rcG-CSFI; space group C2) contains one molecule in the asymmetric unit while form II canine G-CSF (rcG-CSFII; space group P2(1)) has two molecules in the asymmetric unit and bovine G-CSF (rbG-CSF; space group P2(1)2(1)2(1)) contains one molecule in the asymmetric unit. rcG-CSFI has been refined to an R factor of 20.7% with data to 2.3 A resolution and rcG-CSFII has been refined to an R factor of 19.3% with data to 2.2 A resolution. rbG-CSF has been refined to an R factor of 21.3% with data to 1.7 A resolution. The structure of human, canine and bovine G-CSF is an antiparallel 4-alpha-helical bundle with up-up-down-down connectivity. With the exception of one highly exposed loop (residues 66 to 74), the human, canine and bovine structures are very similar to each other. Using our series of G-CSF crystal structures we developed a function that describes the probability that a particular residue position (i) contributes to a G-CSF receptor binding site based on two principles, (1) high sequence conservation in the primary sequence of human, bovine, canine and murine G-CSF and (2) conservation of high solvent accessibility in the human, bovine and canine crystal structures. On the basis of this probability function as well as a comparison of G-CSF to the crystal structure of human growth hormone (hGH) complexed with the extracellular domain of the human growth hormone receptor (hGHbp), residues that contribute to potential G-CSF receptor binding sites are identified.

PubMed: 7504736
DOI: 10.1006/jmbi.1993.1617

Experimental method

X-RAY DIFFRACTION (2.2 Å)