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PDBsum entry 1bfg

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protein links
Growth factor PDB id
1bfg
Jmol
Contents
Protein chain
126 a.a. *
Waters ×99
* Residue conservation analysis
PDB id:
1bfg
Name: Growth factor
Title: Crystal structure of basic fibroblast growth factor at 1.6 angstroms resolution
Structure: Basic fibroblast growth factor. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
1.60Å     R-factor:   0.153    
Authors: Y.Kitagawa,H.Ago,Y.Katsube,A.Fujishima,Y.Matsuura
Key ref: H.Ago et al. (1991). Crystal structure of basic fibroblast growth factor at 1.6 A resolution. J Biochem, 110, 360-363. PubMed id: 1769963
Date:
15-Apr-93     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P09038  (FGF2_HUMAN) -  Fibroblast growth factor 2
Seq:
Struc:
288 a.a.
126 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     fibroblast growth factor receptor signaling pathway   1 term 
  Biochemical function     receptor binding     3 terms  

 

 
J Biochem 110:360-363 (1991)
PubMed id: 1769963  
 
 
Crystal structure of basic fibroblast growth factor at 1.6 A resolution.
H.Ago, Y.Kitagawa, A.Fujishima, Y.Matsuura, Y.Katsube.
 
  ABSTRACT  
 
We have determined the crystal structures of two types of human basic fibroblast growth factor, the serine analogue and the wild-type, at 1.6 and 2.5 A resolution, respectively. Two good heavy atom derivatives were found and used for multiple isomorphous replacement phasing. The atomic coordinates were refined using the Hendrickson & Konnert program for stereochemically restrained refinement against structure factors. The crystallographic R factors were reduced to 15.3% for the serine analogue structure and 16.0% for the wild-type structure. The serine analogue and wild-type structures have been found to be almost identical, the root-mean-square deviation between the corresponding C alpha atoms being 0.11 A. Their structures are composed of twelve beta-strands forming a barrel and three loops. Their molecules have an approximate threefold internal symmetry and are similar in architecture to that of interleukin-1 beta. A possible heparin-binding site, which comprises five basic residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by calculating the electrostatic potential energy.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19846555 M.Renko, J.Sabotic, M.Mihelic, J.Brzin, J.Kos, and D.Turk (2010).
Versatile loops in mycocypins inhibit three protease families.
  J Biol Chem, 285, 308-316.
PDB codes: 3h6q 3h6r 3h6s
19560816 U.Freudenberg, A.Hermann, P.B.Welzel, K.Stirl, S.C.Schwarz, M.Grimmer, A.Zieris, W.Panyanuwat, S.Zschoche, D.Meinhold, A.Storch, and C.Werner (2009).
A star-PEG-heparin hydrogel platform to aid cell replacement therapies for neurodegenerative diseases.
  Biomaterials, 30, 5049-5060.  
  15543670 Q.Zhang, G.J.Wang, and J.G.Sun (2004).
Pharmacokinetics of recombinant human basic fibroblast growth factor in mice using a radioiodination method combined with SDS-PAGE and a sandwich enzyme-linked immunosorbent assay.
  Eur J Drug Metab Pharmacokinet, 29, 163-168.  
11223514 H.J.Hecht, R.Adar, B.Hofmann, O.Bogin, H.Weich, and A.Yayon (2001).
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.
  Acta Crystallogr D Biol Crystallogr, 57, 378-384.
PDB code: 1g82
11714927 S.R.Brych, S.I.Blaber, T.M.Logan, and M.Blaber (2001).
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
  Protein Sci, 10, 2587-2599.
PDB codes: 1jqz 1jt3 1jt4 1jt5 1jt7 1jtc
10413500 K.M.Patrie, M.J.Botelho, K.Franklin, and I.M.Chiu (1999).
Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1.
  Biochemistry, 38, 9264-9272.  
9636026 P.J.Kim, K.Sakaguchi, H.Sakamoto, C.Saxinger, R.Day, P.McPhie, J.S.Rubin, and D.P.Bottaro (1998).
Colocalization of heparin and receptor binding sites on keratinocyte growth factor.
  Biochemistry, 37, 8853-8862.  
9818261 S.Faham, R.J.Linhardt, and D.C.Rees (1998).
Diversity does make a difference: fibroblast growth factor-heparin interactions.
  Curr Opin Struct Biol, 8, 578-586.  
9125499 F.J.Moy, M.Safran, A.P.Seddon, D.Kitchen, P.Böhlen, D.Aviezer, A.Yayon, and R.Powers (1997).
Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor.
  Biochemistry, 36, 4782-4791.  
8968609 B.S.Chang, R.M.Beauvais, T.Arakawa, L.O.Narhi, A.Dong, D.I.Aparisio, and J.F.Carpenter (1996).
Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution.
  Biophys J, 71, 3399-3406.  
8885834 F.J.Moy, A.P.Seddon, P.Böhlen, and R.Powers (1996).
High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.
  Biochemistry, 35, 13552-13561.
PDB codes: 1bla 1bld
8570646 G.Venkataraman, V.Sasisekharan, A.B.Herr, D.M.Ornitz, G.Waksman, C.L.Cooney, R.Langer, and R.Sasisekharan (1996).
Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation.
  Proc Natl Acad Sci U S A, 93, 845-850.  
8790420 P.M.Smallwood, I.Munoz-Sanjuan, P.Tong, J.P.Macke, S.H.Hendry, D.J.Gilbert, N.G.Copeland, N.A.Jenkins, and J.Nathans (1996).
Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development.
  Proc Natl Acad Sci U S A, 93, 9850-9857.  
8610159 Y.Kato, T.Muto, T.Tomura, H.Tsumura, H.Watarai, T.Mikayama, K.Ishizaka, and R.Kuroki (1996).
The crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded beta-sheets.
  Proc Natl Acad Sci U S A, 93, 3007-3010.
PDB code: 1gif
8590594 T.Arakawa, P.Holst, L.O.Narhi, J.S.Philo, J.Wen, S.J.Prestrelski, X.Zhu, D.C.Rees, and G.M.Fox (1995).
The importance of Arg40 and 45 in the mitogenic activity and structural stability of basic fibroblast growth factor: effects of acidic amino acid substitutions.
  J Protein Chem, 14, 263-274.  
8024698 D.F.Kusewitt, C.L.Sabourin, C.L.Budge, T.E.Sherburn, and R.D.Ley (1994).
Characterization of cDNA encoding basic fibroblast growth factor of the marsupial Monodelphis domestica.
  DNA Cell Biol, 13, 549-554.  
  7691311 A.E.Eriksson, L.S.Cousens, and B.W.Matthews (1993).
Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
  Protein Sci, 2, 1274-1284.
PDB codes: 1fga 4fgf
7520817 X.Zhu, B.T.Hsu, and D.C.Rees (1993).
Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor.
  Structure, 1, 27-34.
PDB code: 1afc
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 codes are shown on the right.