PDBsum entry 1epj

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protein links
Growth factor PDB id
Protein chain
53 a.a. *
* Residue conservation analysis
PDB id:
Name: Growth factor
Title: Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological ph solutions
Structure: Epidermal growth factor. Chain: a. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090
NMR struc: 5 models
Authors: D.Kohda,F.Inagaki
Key ref:
D.Kohda and F.Inagaki (1992). Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Biochemistry, 31, 11928-11939. PubMed id: 1445923 DOI: 10.1021/bi00162a036
24-Mar-92     Release date:   31-Jan-94    
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Protein chain
Pfam   ArchSchema ?
P01132  (EGF_MOUSE) -  Pro-epidermal growth factor
1217 a.a.
53 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain


DOI no: 10.1021/bi00162a036 Biochemistry 31:11928-11939 (1992)
PubMed id: 1445923  
Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions.
D.Kohda, F.Inagaki.
The three-dimensional structures of epidermal growth factors (EGF) previously reported were all in acidic solutions (pH 2.0-3.2), at which pHs EGF cannot bind to the receptor. Here we studied the structure of mouse EGF at pH 6.8, where EGF is physiologically active, and compared it with the structure at pH 2.0 by CD and NMR. From pH dependence of CD spectra and a comparison between the chemical shifts of the proton resonances at pH 6.8 and 2.0, the conformations at two pHs were found to be nearly identical except for the C-terminal tail region. The three-dimensional structures at pH 6.8 and 2.0 were determined independently by a combination of two-dimensional 1H NMR and stimulated annealing calculations using the program XPLOR. The calculations were based on 261 distance constraints at pH 6.8 and 355 distance and 24 torsion angle constraints at pH 2.0. The conformational difference of the C-terminal domain (residues 33-50) was detected between the two structures, which were supported by CD and the chemical shift comparison. The positions of the side chains of Leu47, Arg48, Trp49, and Trp50 are changed probably by the effect of the deprotonation of Asp46. Considering the fact that Leu47 is essential in EGF binding to the receptor, this conformational difference may be important in receptor recognition.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20208353 K.Nagata (2010).
Studies of the structure-activity relationships of peptides and proteins involved in growth and development based on their three-dimensional structures.
  Biosci Biotechnol Biochem, 74, 462-470.  
19896952 Q.Guo, M.Manolopoulou, Y.Bian, A.B.Schilling, and W.J.Tang (2010).
Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme.
  J Mol Biol, 395, 430-443.
PDB codes: 2wk3 3e4z 3e50 3hgz
19531495 Y.Liu, D.S.Annis, and D.F.Mosher (2009).
Interactions among the epidermal growth factor-like modules of thrombospondin-1.
  J Biol Chem, 284, 22206-22212.  
18199660 I.Iloro, D.Narváez, N.Guillén, C.M.Camacho, L.Guillén, E.Cora, and B.Pastrana-Ríos (2008).
The kinetics of the hydrogen/deuterium exchange of epidermal growth factor receptor ligands.
  Biophys J, 94, 4041-4055.  
12297050 H.Ogiso, R.Ishitani, O.Nureki, S.Fukai, M.Yamanaka, J.H.Kim, K.Saito, A.Sakamoto, M.Inoue, M.Shirouzu, and S.Yokoyama (2002).
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
  Cell, 110, 775-787.
PDB code: 1ivo
11985614 J.H.Kim, K.Saito, and S.Yokoyama (2002).
Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin.
  Eur J Biochem, 269, 2323-2329.  
11964230 M.Martin-Fernandez, D.T.Clarke, M.J.Tobin, S.V.Jones, and G.R.Jones (2002).
Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling.
  Biophys J, 82, 2415-2427.  
12297049 T.P.Garrett, N.M.McKern, M.Lou, T.C.Elleman, T.E.Adams, G.O.Lovrecz, H.J.Zhu, F.Walker, M.J.Frenkel, P.A.Hoyne, R.N.Jorissen, E.C.Nice, A.W.Burgess, and C.W.Ward (2002).
Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
  Cell, 110, 763-773.
PDB code: 1mox
11733021 S.G.Chamberlin, L.Brennan, S.M.Puddicombe, D.E.Davies, and D.L.Turner (2001).
Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor.
  Eur J Biochem, 268, 6247-6255.
PDB code: 1gk5
10666628 J.J.Chai, M.Li, B.R.Huang, Y.Luo, M.Luo, R.C.Bi, and C.H.He (2000).
Crystallization and preliminary X-ray diffraction studies of human epidermal growth factor.
  Acta Crystallogr D Biol Crystallogr, 56, 62-63.  
  10716183 R.N.Jorissen, V.C.Epa, H.R.Treutlein, T.P.Garrett, C.W.Ward, and A.W.Burgess (2000).
Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor.
  Protein Sci, 9, 310-324.
PDB codes: 1dnq 1dnr
10704223 T.A.Ramelot, L.N.Gentile, and L.K.Nicholson (2000).
Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors.
  Biochemistry, 39, 2714-2725.  
10103060 P.Ascenzi, M.Ruoppolo, A.Amoresano, P.Pucci, R.Consonni, L.Zetta, S.Pascarella, F.Bortolotti, and E.Menegatti (1999).
Characterization of low-molecular-mass trypsin isoinhibitors from oil-rape (Brassica napus var. oleifera) seed.
  Eur J Biochem, 261, 275-284.  
9890941 T.Aizawa, N.Fujitani, Y.Hayakawa, A.Ohnishi, T.Ohkubo, Y.Kumaki, K.Kawano, K.Hikichi, and K.Nitta (1999).
Solution structure of an insect growth factor, growth-blocking peptide.
  J Biol Chem, 274, 1887-1890.
PDB code: 1bqf
  10082370 K.J.Barnham, A.M.Torres, D.Alewood, P.F.Alewood, T.Domagala, E.C.Nice, and R.S.Norton (1998).
Role of the 6-20 disulfide bridge in the structure and activity of epidermal growth factor.
  Protein Sci, 7, 1738-1749.
PDB code: 1a3p
8702666 A.E.Summerfield, A.K.Hudnall, T.J.Lukas, C.A.Guyer, and J.V.Staros (1996).
Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor.
  J Biol Chem, 271, 19656-19659.  
8824265 J.Nelson, W.N.Scott, W.E.Allen, D.J.Wilson, P.Harriott, N.V.McFerran, and B.Walker (1996).
Murine epidermal growth factor peptide (33-42) binds to a YIGSR-specific laminin receptor on both tumor and endothelial cells.
  J Biol Chem, 271, 26179-26186.  
8747437 C.C.Lester, B.Wang, R.Wu, and H.A.Scheraga (1995).
Structure-function studies of mEGF: probing the type I beta-turn between residues 25 and 26.
  J Protein Chem, 14, 753-762.  
  7527339 H.Terasawa, D.Kohda, H.Hatanaka, K.Nagata, N.Higashihashi, H.Fujiwara, K.Sakano, and F.Inagaki (1994).
Solution structure of human insulin-like growth factor II; recognition sites for receptors and binding proteins.
  EMBO J, 13, 5590-5597.  
  8062828 K.Nagata, D.Kohda, H.Hatanaka, S.Ichikawa, S.Matsuda, T.Yamamoto, A.Suzuki, and F.Inagaki (1994).
Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4.
  EMBO J, 13, 3517-3523.
PDB codes: 1hre 1hrf
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.