1bgd: Difference between revisions

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

OverviewOverview

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.

About this StructureAbout this Structure

1BGD is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF)., Lovejoy B, Cascio D, Eisenberg D, J Mol Biol. 1993 Dec 5;234(3):640-53. PMID:7504736

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 '''CRYSTAL STRUCTURE OF CANINE AND BOVINE GRANULOCYTE-COLONY STIMULATING FACTOR (G-CSF)'''<br />
 ==Overview==
-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 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.
 ==About this Structure==
-BGD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BGD OCA].
+BGD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGD OCA].
 ==Reference==
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 [[Category: cytokine]]
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