Abstract
The epidermal growth factors (EGFs)1–3are powerful mitogens for a wide variety of cells in culture4; human EGF (hEGF), known as urogastrone, also inhibits gastric acid secretion in vivo1. The transforming growth factors (TGF-α) are related to the EGF family both in sequence5 and activity6,7and EGF-like sequences are often observed in a wide range of functionally unrelated proteins8. 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.
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Cooke, R., Wilkinson, A., Baron, M. et al. The solution structure of human epidermal growth factor. Nature 327, 339–341 (1987). https://doi.org/10.1038/327339a0
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DOI: https://doi.org/10.1038/327339a0
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