Structure-function relationships in epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
The solution structures of the homologous growth factors human epidermal growth factor (hEGF) and human transforming growth factor-alpha (hTGF-alpha), as determined by high resolution NMR and various computational methods, are described. Knowledge of these structures and the sequences of other homologous proteins leads to predictions about growth factor residues which may be involved in the receptor/ligand interface. Recent experiments designed to check these predictions are described briefly. These involve site-specific mutagenesis, receptor binding assays and high resolution NMR studies.
Campbell
I D
ID
Department of Biochemistry, University of Oxford, U.K.
Baron
M
M
Cooke
R M
RM
Dudgeon
T J
TJ
Fallon
A
A
Harvey
T S
TS
Tappin
M J
MJ
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003198:Computer Simulation; D004815:Epidermal Growth Factor / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D015291:Transforming Growth Factors / Q000378:metabolism
D004815:Epidermal Growth Factor; D015291:Transforming Growth Factors