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PDBsum entry 1bge

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protein Protein-protein interface(s) links
Cytokine PDB id
1bge
Jmol
Contents
Protein chains
159 a.a. *
Waters ×399
* Residue conservation analysis
PDB id:
1bge
Name: Cytokine
Title: Crystal structure of canine and bovine granulocyte-colony stimulating factor (g-csf)
Structure: Granulocyte colony-stimulating factor. Chain: a, b. Engineered: yes
Source: Canis lupus familiaris. Dog. Organism_taxid: 9615. Strain: familiaris
Resolution:
2.20Å     R-factor:   0.193    
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P35834  (CSF3_CANFA) -  Granulocyte colony-stimulating factor
Seq:
Struc:
175 a.a.
159 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     immune response   1 term 
  Biochemical function     cytokine activity     2 terms  

 

 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17704182 W.F.Weiss, T.K.Hodgdon, E.W.Kaler, A.M.Lenhoff, and C.J.Roberts (2007).
Nonnative protein polymers: structure, morphology, and relation to nucleation and growth.
  Biophys J, 93, 4392-4403.  
16963649 L.H.Lucas, B.A.Ersoy, L.A.Kueltzo, S.B.Joshi, D.T.Brandau, N.Thyagarajapuram, L.J.Peek, and C.R.Middaugh (2006).
Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions.
  Protein Sci, 15, 2228-2243.  
16597829 R.S.Rajan, T.Li, M.Aras, C.Sloey, W.Sutherland, H.Arai, R.Briddell, O.Kinstler, A.M.Lueras, Y.Zhang, H.Yeghnazar, M.Treuheit, and D.N.Brems (2006).
Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study.
  Protein Sci, 15, 1063-1075.  
12712430 C.J.Roberts, R.T.Darrington, and M.B.Whitley (2003).
Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life.
  J Pharm Sci, 92, 1095-1111.  
12949999 L.A.Kueltzo, B.Ersoy, J.P.Ralston, and C.R.Middaugh (2003).
Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: a bGCSF case study.
  J Pharm Sci, 92, 1805-1820.  
12949998 L.A.Kueltzo, and C.R.Middaugh (2003).
Structural characterization of bovine granulocyte colony stimulating factor: effect of temperature and pH.
  J Pharm Sci, 92, 1793-1804.  
11967378 P.Luo, R.J.Hayes, C.Chan, D.M.Stark, M.Y.Hwang, J.M.Jacinto, P.Juvvadi, H.S.Chung, A.Kundu, M.L.Ary, and B.I.Dahiyat (2002).
Development of a cytokine analog with enhanced stability using computational ultrahigh throughput screening.
  Protein Sci, 11, 1218-1226.  
11485185 K.Kasraian, A.Kuzniar, D.Earley, B.J.Kamicker, G.Wilson, T.Manion, J.Hong, C.Reiber, and P.Canning (2001).
Sustained in vivo activity of recombinant bovine granulocyte colony stimulating factor (rbG-CSF) using HEPES buffer.
  Pharm Dev Technol, 6, 441-447.  
10194378 C.A.McWherter, Y.Feng, L.L.Zurfluh, B.K.Klein, M.P.Baganoff, J.O.Polazzi, W.F.Hood, K.Paik, A.L.Abegg, E.S.Grabbe, J.J.Shieh, A.M.Donnelly, and J.P.McKearn (1999).
Circular permutation of the granulocyte colony-stimulating factor receptor agonist domain of myelopoietin.
  Biochemistry, 38, 4564-4571.  
10364174 J.E.Layton, G.Shimamoto, T.Osslund, A.Hammacher, D.K.Smith, H.R.Treutlein, and T.Boone (1999).
Interaction of granulocyte colony-stimulating factor (G-CSF) with its receptor. Evidence that Glu19 of G-CSF interacts with Arg288 of the receptor.
  J Biol Chem, 274, 17445-17451.  
10194377 Y.Feng, J.C.Minnerly, L.L.Zurfluh, W.D.Joy, W.F.Hood, A.L.Abegg, E.S.Grabbe, J.J.Shieh, T.L.Thurman, J.P.McKearn, and C.A.McWherter (1999).
Circular permutation of granulocyte colony-stimulating factor.
  Biochemistry, 38, 4553-4563.  
9472779 M.A.Peirone, K.Delaney, J.Kwiecin, A.Fletch, and P.L.Chang (1998).
Delivery of recombinant gene product to canines with nonautologous microencapsulated cells.
  Hum Gene Ther, 9, 195-206.  
  9194183 D.C.Young, H.Zhan, Q.L.Cheng, J.Hou, and D.J.Matthews (1997).
Characterization of the receptor binding determinants of granulocyte colony stimulating factor.
  Protein Sci, 6, 1228-1236.  
9254611 D.H.Purvis, and B.C.Mabbutt (1997).
Solution dynamics and secondary structure of murine leukemia inhibitory factor: a four-helix cytokine with a rigid CD loop.
  Biochemistry, 36, 10146-10154.  
9166791 J.M.Matthews, L.D.Ward, A.Hammacher, R.S.Norton, and R.J.Simpson (1997).
Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6.
  Biochemistry, 36, 6187-6196.  
  9144766 R.J.Simpson, A.Hammacher, D.K.Smith, J.M.Matthews, and L.D.Ward (1997).
Interleukin-6: structure-function relationships.
  Protein Sci, 6, 929-955.  
9118960 W.Somers, M.Stahl, and J.S.Seehra (1997).
1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling.
  EMBO J, 16, 989-997.
PDB code: 1alu
8703906 J.F.Reidhaar-Olson, J.A.De Souza-Hart, and H.E.Selick (1996).
Identification of residues critical to the activity of human granulocyte colony-stimulating factor.
  Biochemistry, 35, 9034-9041.  
8884748 M.Inoue, C.Nakayama, and H.Noguchi (1996).
Activating mechanism of CNTF and related cytokines.
  Mol Neurobiol, 12, 195-209.  
8784206 V.De Filippis, P.P.de Laureto, N.Toniutti, and A.Fontana (1996).
Acid-induced molten globule state of a fully active mutant of human interleukin-6.
  Biochemistry, 35, 11503-11511.  
7773741 H.R.Mott, and I.D.Campbell (1995).
Four-helix bundle growth factors and their receptors: protein-protein interactions.
  Curr Opin Struct Biol, 5, 114-121.  
  7613464 M.H.Seto, R.N.Harkins, M.Adler, M.Whitlow, W.B.Church, and E.Croze (1995).
Homology model of human interferon-alpha 8 and its receptor complex.
  Protein Sci, 4, 655-670.  
  7520794 E.Demchuk, T.Mueller, H.Oschkinat, W.Sebald, and R.C.Wade (1994).
Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis.
  Protein Sci, 3, 920-935.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.