The solution structure of human epidermal growth factor
摘要：
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. The transforming growth factors (TGF-α) are related to the EGF family both in sequenceand activityand 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 resolutionH 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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关键词：
BACKSCATTERED ELECTRON IMAGING MICRORADIOGRAPHY PROJECTION EFFECT ERRORS HISTOMETRY MINERAL CONTENT, BONE, SCANNING ELECTRON MICROSCOPE, CORTICAL, CANCELLOUS, MORPHOLOGY
DOI：
10.1038/327339a0
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