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Growth factor PDB id
2gmf
Jmol
Contents
Protein chains
121 a.a. *
Waters ×92
* Residue conservation analysis
PDB id:
2gmf
Name: Growth factor
Title: Human granulocyte macrophage colony stimulating factor
Structure: Granulocyte-macrophage colony-stimulating factor. Chain: a, b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.40Å     R-factor:   0.235    
Authors: D.Rozwarski,K.Diederichs,R.Hecht,T.Boone,P.A.Karplus
Key ref: D.A.Rozwarski et al. (1996). Refined crystal structure and mutagenesis of human granulocyte-macrophage colony-stimulating factor. Proteins, 26, 304-313. PubMed id: 8953651 DOI: 10.1002/(SICI)1097-0134(199611)26:3<304::AID-PROT6>3.0.CO;2-D
Date:
24-Apr-96     Release date:   08-Nov-96    
Supersedes: 1gmf
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04141  (CSF2_HUMAN) -  Granulocyte-macrophage colony-stimulating factor
Seq:
Struc: 		144 a.a.
121 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     positive regulation of podosome assembly   16 terms 
  Biochemical function     protein binding     4 terms  

 

 
DOI no: 10.1002/(SICI)1097-0134(199611)26:3<304::AID-PROT6>3.0.CO;2-D Proteins 26:304-313 (1996)
PubMed id: 8953651  
 
 
Refined crystal structure and mutagenesis of human granulocyte-macrophage colony-stimulating factor.
D.A.Rozwarski, K.Diederichs, R.Hecht, T.Boone, P.A.Karplus.
 
  ABSTRACT  
 
The crystal structure of recombinant human granulocyte-macrophage colony stimulating factor (rhGM-CSF) has been refined against data extending to a resolution of approximately 2.4 A along a* and approximately 1.9 A along b* and c*. Anisotropic scale factors of B11 = -20.8 A2, B22 = 7.4 A2, B33 = 13.3 A2 corrected for the more rapid fall of diffraction in the a* direction. The anisotropy correlates with the weak crystal packing interactions along the a axis. In addition to apolar side chains in the protein core, there are 10 buried hydrogen bonding residues. Those residues involved in intramolecular hydrogen bonding to main chain atoms are better conserved than those hydrogen bonding to other side chain atoms; 24 solvation sites are observed at equivalent positions in the two molecules in the asymmetric unit, and the strongest among these are located in clefts between secondary structural elements. No buried water sites are seen. Two surface clusters of hydrophobic side chains are located near the expected receptor binding regions. Mutagenesis of 11 residues on the helix A/helix C face confirms the importance of Glu-21 and shows that Gly-75 and Gln-86, located on helix C, each cause a greater than fourfold drop in activity. Glu-21 and Gly-75, but not Gln-86, are structurally equivalent to residues involved in the growth hormone binding to its receptor.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20179338 T.C.Terwilliger (2010).
Rapid model building of alpha-helices in electron-density maps.
  Acta Crystallogr D Biol Crystallogr, 66, 268-275.  
20179339 T.C.Terwilliger (2010).
Rapid model building of beta-sheets in electron-density maps.
  Acta Crystallogr D Biol Crystallogr, 66, 276-284.  
20179340 T.C.Terwilliger (2010).
Rapid chain tracing of polypeptide backbones in electron-density maps.
  Acta Crystallogr D Biol Crystallogr, 66, 285-294.  
19352505 R.Dey, K.Ji, Z.Liu, and L.Chen (2009).
A cytokine-cytokine interaction in the assembly of higher-order structure and activation of the interleukine-3:receptor complex.
  PLoS ONE, 4, e5188.  
19436055 T.R.Hercus, D.Thomas, M.A.Guthridge, P.G.Ekert, J.King-Scott, M.W.Parker, and A.F.Lopez (2009).
The granulocyte-macrophage colony-stimulating factor receptor: linking its structure to cell signaling and its role in disease.
  Blood, 114, 1289-1298.  
18692472 G.Hansen, T.R.Hercus, B.J.McClure, F.C.Stomski, M.Dottore, J.Powell, H.Ramshaw, J.M.Woodcock, Y.Xu, M.Guthridge, W.J.McKinstry, A.F.Lopez, and M.W.Parker (2008).
The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation.
  Cell, 134, 496-507.
PDB code: 3cxe
16929102 R.Pai, J.Sacchettini, and T.Ioerger (2006).
Identifying non-crystallographic symmetry in protein electron-density maps: a feature-based approach.
  Acta Crystallogr D Biol Crystallogr, 62, 1012-1021.  
16173810 D.H.Doherty, M.S.Rosendahl, D.J.Smith, J.M.Hughes, E.A.Chlipala, and G.N.Cox (2005).
Site-specific PEGylation of engineered cysteine analogues of recombinant human granulocyte-macrophage colony-stimulating factor.
  Bioconjug Chem, 16, 1291-1298.  
11747625 L.Runkel, C.De Dios, M.Karpusas, D.Baker, Z.Li, M.Zafari, M.Betzenhauser, C.Muldowney, S.Miller, P.N.Redlich, S.E.Grossberg, A.Whitty, and P.S.Hochman (2001).
Mapping of IFN-beta epitopes important for receptor binding and biologic activation: comparison of results achieved using antibody-based methods and alanine substitution mutagenesis.
  J Interferon Cytokine Res, 21, 931-941.  
  11155818 A.E.Frankel, E.L.Sievers, and D.A.Scheinberg (2000).
Cell surface receptor-targeted therapy of acute myeloid leukemia: a review.
  Cancer Biother Radiopharm, 15, 459-476.  
  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.  
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.