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PDBsum entry 1yuf

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protein links
Growth factor PDB id
1yuf
Jmol
Contents
Protein chain
50 a.a. *
* Residue conservation analysis
PDB id:
1yuf
Name: Growth factor
Title: Type alpha transforming growth factor, nmr, 16 models without energy minimization
Structure: Transforming growth factor alpha. Chain: a. Synonym: tgf-alpha, h-tgf-alpha. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: human tgf-alpha 1yuf. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 16 models
Authors: F.J.Moy,G.T.Montelione,H.A.Scheraga
Key ref:
F.J.Moy et al. (1993). Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints. Biochemistry, 32, 7334-7353. PubMed id: 8338831 DOI: 10.1021/bi00080a003
Date:
01-Apr-96     Release date:   17-Aug-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 

 
DOI no: 10.1021/bi00080a003 Biochemistry 32:7334-7353 (1993)
PubMed id: 8338831  
 
 
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
F.J.Moy, Y.C.Li, P.Rauenbuehler, M.E.Winkler, H.A.Scheraga, G.T.Montelione.
 
  ABSTRACT  
 
Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein containing 50 amino acids and 3 disulfide bonds. Homo- and heteronuclear NMR spectra were used to determine nearly complete sequence-specific 1H and 15N resonance assignments for hTGF alpha under three conditions: pH 6.5 and a temperature of 10 degrees C, pH 6.5 and a temperature of 30 degrees C, and pH 3.5 and a temperature of 30 degrees C. The 15N-enriched samples of hTGF alpha allowed determination of many 3J(HN-H alpha) vicinal coupling constants. Solution structures of human type-alpha transforming growth factor (hTGF alpha) at pH 6.5 and a temperature of 10 degrees C were determined from NMR data using molecular structure generation calculations and restrained energy minimization. These structures are based on 425 conformational constraints, including 357 NOE-derived upper-bound distance constraints, constraints on the ranges of 26 dihedral angles based on measurements of vicinal coupling constants, 42 upper- and lower-bound constraints associated with 6 hydrogen bonds and 3 disulfide bonds, and several stereospecific 1H resonance assignments. The overall structure is similar to that described recently for hTGF alpha by other groups [Kline et al. (1990) Biochemistry 29, 7805-7813; Harvey et al. (1991). Eur. J. Biochem. 198, 555-562], but there are differences in some structural details. The resonance frequencies, vicinal coupling constants, and NOEs form the basis for comparisons of the solution structure of hTGF alpha at neutral and acidic pH. At pH 3.5 the protein structure is partially disordered, with most of the hydrogen-bonded backbone structure still intact. The hTGF alpha structure is also compared with that of murine epidermal growth factor. Coordinates for the set of hTGF alpha structures described in this paper have been deposited in the Protein Data Bank.
 

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.  
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
14517980 W.Li, Y.Zhang, D.Kihara, Y.J.Huang, D.Zheng, G.T.Montelione, A.Kolinski, and J.Skolnick (2003).
TOUCHSTONEX: protein structure prediction with sparse NMR data.
  Proteins, 53, 290-306.  
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
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.  
9636055 D.Tolkatchev, and F.Ni (1998).
Calcium binding properties of an epidermal growth factor-like domain from human thrombomodulin.
  Biochemistry, 37, 9091-9100.  
9566117 C.McInnes, and B.D.Sykes (1997).
Growth factor receptors: structure, mechanism, and drug discovery.
  Biopolymers, 43, 339-366.  
8816772 C.E.White, M.J.Hunter, D.P.Meininger, S.Garrod, and E.A.Komives (1996).
The fifth epidermal growth factor-like domain of thrombomodulin does not have an epidermal growth factor-like disulfide bonding pattern.
  Proc Natl Acad Sci U S A, 93, 10177-10182.  
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.  
8555177 L.Jendeberg, M.Tashiro, R.Tejero, B.A.Lyons, M.Uhlén, G.T.Montelione, and B.Nilsson (1996).
The mechanism of binding staphylococcal protein A to immunoglobin G does not involve helix unwinding.
  Biochemistry, 35, 22-31.
PDB code: 1spz
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.  
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.  
  8528067 D.P.Meininger, M.J.Hunter, and E.A.Komives (1995).
Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin.
  Protein Sci, 4, 1683-1695.
PDB code: 1zaq
  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.  
  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.