The solution structure of human epidermal growth factor.
The epidermal growth factors (EGFs) are powerful mitogens for a wide variety of cells in culture; human EGF (hEGF), known as urogastrone, also inhibits gastric acid secretion in vivo. The transforming growth factors (TGF-alpha) are related to the EGF family both in sequence and activity and EGF-like sequences are often observed in a wide range of functionally unrelated proteins. Attempts to examine the structure of EGF by diffraction methods have not yet succeeded because of difficulties with crystallization. We report here a three-dimensional structure of a biologically active derivative (residues 1-48) of the 53-residue human EGF. An analysis of high resolution 1H nuclear magnetic resonance (NMR) spectra was used together with a combination of distance geometry, restrained energy minimization and restrained molecular dynamics methods. The three-dimensional structure provides a basis for understanding the properties of EGFs and for predicting the structures of homologous sequences in other proteins.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003201:Computers; D004220:Disulfides; D004815:Epidermal Growth Factor; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D055585:Physical Phenomena; D010825:Physics; D011487:Protein Conformation; D012996:Solutions
D004220:Disulfides; D012996:Solutions; D004815:Epidermal Growth Factor