1bgd: Difference between revisions

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[[Image:1bgd.gif|left|200px]]
[[Image:1bgd.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgd OCA], [http://www.ebi.ac.uk/pdbsum/1bgd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bgd RCSB]</span>
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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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[[Category: Eisenberg, D.]]
[[Category: Eisenberg, D.]]
[[Category: Lovejoy, B.]]
[[Category: Lovejoy, B.]]
[[Category: cytokine]]
[[Category: Cytokine]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:28:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:20 2008''

Revision as of 11:28, 2 May 2008

File:1bgd.gif

Template:STRUCTURE 1bgd

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 Page seeded by OCA on Fri May 2 11:28:43 2008

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