PDBsum entry 1bgd

Cytokine

PDB id: 1bgd

Contents

Protein chain

157 a.a. *

Waters ×174

* Residue conservation analysis

PDB id:

1bgd

Name:

Cytokine

Title:

Crystal structure of canine and bovine granulocyte-colony stimulating factor (g-csf)

Structure:

Granulocyte colony-stimulating factor. Chain: a. Engineered: yes

Source:

Canis lupus familiaris. Dog. Organism_taxid: 9615. Strain: familiaris

Resolution:

2.30Å R-factor: 0.207

Authors:

B.Lovejoy,D.Cascio,D.Eisenberg

Key ref:

B.Lovejoy et al. (1993). Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF). J Mol Biol, 234, 640-653. PubMed id: 7504736

Date:

27-Apr-93 Release date: 31-Oct-93

Protein chain

P35834  (CSF3_CANLF) -  Granulocyte colony-stimulating factor from Canis lupus familiaris

Seq: 175 a.a.

Struc: 157 a.a.

J Mol Biol 234:640-653 (1993)

PubMed id: 7504736

Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF).

B.Lovejoy, D.Cascio, D.Eisenberg.

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.