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PDBsum entry 2tgf

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Growth factor PDB id
2tgf

 

 

 

 

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Contents
Protein chain
50 a.a. *
* Residue conservation analysis
PDB id:
2tgf
Name: Growth factor
Title: The solution structure of human transforming growth factor alpha
Structure: Transforming growth factor-alpha. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 1 models
Authors: T.S.Harvey,A.J.Wilkinson,M.J.Tappin,R.M.Cooke,I.D.Campbell
Key ref: T.S.Harvey et al. (1991). The solution structure of human transforming growth factor alpha. Eur J Biochem, 198, 555-562. PubMed id: 2050136
Date:
23-Jan-91     Release date:   15-Apr-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01135  (TGFA_HUMAN) -  Protransforming growth factor alpha from Homo sapiens
Seq:
Struc:
160 a.a.
50 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Eur J Biochem 198:555-562 (1991)
PubMed id: 2050136  
 
 
The solution structure of human transforming growth factor alpha.
T.S.Harvey, A.J.Wilkinson, M.J.Tappin, R.M.Cooke, I.D.Campbell.
 
  ABSTRACT  
 
The solution structure of transforming growth factor alpha has been determined by a combination of high-resolution 1H-nuclear magnetic resonance and distance geometry and restrained molecular dynamics. The 382 restraints derived from the NMR experiments were used to calculate many distance geometry structures, which were then refined by restrained molecular mechanics. Five of these structures were further refined using a variety of methods. Comparison of independently measured parameters, such as calculated hydrogen bonding patterns and experimental amide exchange rates, have been used to evaluate the accuracy of the structures. Also, possible mechanisms to explain the pH-dependent conformational interconversion observed are suggested. Finally comparisons between this work and others on this topic have been made.
 

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
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.  
  19662225 J.M.Kneller, T.Ehlen, J.P.Matisic, D.Miller, D.Van Niekerk, W.L.Lam, M.Marra, R.Richards-Kortum, M.Follen, C.Macaulay, and S.J.Jones (2007).
Using LongSAGE to Detect Biomarkers of Cervical Cancer Potentially Amenable to Optical Contrast Agent Labelling.
  Biomark Insights, 2, 447-461.  
12869572 M.Wingens, T.Walma, H.van Ingen, C.Stortelers, J.E.van Leeuwen, E.J.van Zoelen, and G.W.Vuister (2003).
Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity.
  J Biol Chem, 278, 39114-39123.
PDB code: 1p9j
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
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
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.  
9692950 A.Muranyi, B.E.Finn, G.P.Gippert, S.Forsén, J.Stenflo, and T.Drakenberg (1998).
Solution structure of the N-terminal EGF-like domain from human factor VII.
  Biochemistry, 37, 10605-10615.
PDB code: 1bf9
9477945 B.Bersch, J.F.Hernandez, D.Marion, and G.J.Arlaud (1998).
Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family.
  Biochemistry, 37, 1204-1214.
PDB code: 1apq
9765263 C.McInnes, J.Wang, A.E.Al Moustafa, C.Yansouni, M.O'Connor-McCourt, and B.D.Sykes (1998).
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
  J Biol Chem, 273, 27357-27363.  
9565587 J.T.Jones, M.D.Ballinger, P.I.Pisacane, J.A.Lofgren, V.D.Fitzpatrick, W.J.Fairbrother, J.A.Wells, and M.X.Sliwkowski (1998).
Binding interaction of the heregulinbeta egf domain with ErbB3 and ErbB4 receptors assessed by alanine scanning mutagenesis.
  J Biol Chem, 273, 11667-11674.  
  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
9566117 C.McInnes, and B.D.Sykes (1997).
Growth factor receptors: structure, mechanism, and drug discovery.
  Biopolymers, 43, 339-366.  
9341148 T.Mitamura, T.Umata, F.Nakano, Y.Shishido, T.Toyoda, A.Itai, H.Kimura, and E.Mekada (1997).
Structure-function analysis of the diphtheria toxin receptor toxin binding site by site-directed mutagenesis.
  J Biol Chem, 272, 27084-27090.  
8943277 C.McInnes, D.W.Hoyt, R.N.Harkins, R.N.Pagila, M.T.Debanne, M.O'Connor-McCourt, and B.D.Sykes (1996).
NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis.
  J Biol Chem, 271, 32204-32211.  
8639490 N.E.Jacobsen, N.Abadi, M.X.Sliwkowski, D.Reilly, N.J.Skelton, and W.J.Fairbrother (1996).
High-resolution solution structure of the EGF-like domain of heregulin-alpha.
  Biochemistry, 35, 3402-3417.
PDB codes: 1hae 1haf
  8845748 R.Tejero, D.Bassolino-Klimas, R.E.Bruccoleri, and G.T.Montelione (1996).
Simulated annealing with restrained molecular dynamics using CONGEN: energy refinement of the NMR solution structures of epidermal and type-alpha transforming growth factors.
  Protein Sci, 5, 578-592.  
8901515 S.J.Freedman, D.G.Sanford, W.W.Bachovchin, B.C.Furie, J.D.Baleja, and B.Furie (1996).
Structure and function of the epidermal growth factor domain of P-selectin.
  Biochemistry, 35, 13733-13744.
PDB code: 1fsb
7559494 M.Adler, M.H.Seto, D.E.Nitecki, J.H.Lin, D.R.Light, and J.Morser (1995).
The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin.
  J Biol Chem, 270, 23366-23372.
PDB code: 1tmr
  8535250 M.J.Hunter, and E.A.Komives (1995).
Thrombin-binding affinities of different disulfide-bonded isomers of the fifth EGF-like domain of thrombomodulin.
  Protein Sci, 4, 2129-2137.  
7552703 S.L.Lin, and R.Nussinov (1995).
A disulphide-reinforced structural scaffold shared by small proteins with diverse functions.
  Nat Struct Biol, 2, 835-837.  
  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
8041758 R.J.Goodson, M.V.Doyle, S.E.Kaufman, and S.Rosenberg (1994).
High-affinity urokinase receptor antagonists identified with bacteriophage peptide display.
  Proc Natl Acad Sci U S A, 91, 7129-7133.  
  1304885 M.Baron, D.G.Norman, T.S.Harvey, P.A.Handford, M.Mayhew, A.G.Tse, G.G.Brownlee, and I.D.Campbell (1992).
The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha.
  Protein Sci, 1, 81-90.
PDB code: 1ixa
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.

 

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