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| {{STRUCTURE_1bgc| PDB=1bgc | SCENE= }} | | {{STRUCTURE_1bgc| PDB=1bgc | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF CANINE AND BOVINE GRANULOCYTE-COLONY STIMULATING FACTOR (G-CSF)'''
| | ===CRYSTAL STRUCTURE OF CANINE AND BOVINE GRANULOCYTE-COLONY STIMULATING FACTOR (G-CSF)=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_7504736}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7504736 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7504736}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lovejoy, B.]] | | [[Category: Lovejoy, B.]] |
| [[Category: Cytokine]] | | [[Category: Cytokine]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:28:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:06:23 2008'' |