The solution structures of epidermal growth factor and transforming growth factor alpha |
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| Affiliation: | 1. Department of Neurosurgery and Neurotraumatolgy, Jagiellonian University Medical College, Kraków, Poland;2. TENSOR—Team of NeuroSurgery-Oriented Research, Jagiellonian University Medical College, Kraków, Poland;3. Faculty of Medicine, Jagiellonian University Medical College, Kraków, Poland;4. Department of Internal and Agricultural Medicine, Laboratory of Translational Medicine, Jagiellonian University Medical College, Kraków, Poland;5. Department of Internal Medicine and Gerontology, Jagiellonian University Medical College, Kraków, Poland;6. AGH University of Science and Technology, Faculty of Computer Science, Electronics and Telecommunications, Kraków, Poland;7. BHF Centre for Research Excellence, Institute of Cardiovascular and Medical Research (ICAMS), University of Glasgow, Glasgow, United Kingdom;1. Servicio de Alergia, Instituto de Investigación Sanitaria-Hospital Universitario de la Princesa, Madrid, Spain;2. Departamento de Parasitología, Facultad de Farmacia, Universidad Complutense de Madrid, Madrid, Spain;1. Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle Upon Tyne, NE2 4HH, UK;2. Aviagen Ltd, Newbridge, Midlothian, EU28 8SZ, UK;2. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China |
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| Abstract: | The structures of human epidermal growth factor (EGF) and human transforming growth factor alpha (TGFα) have been determined in solution using nuclear magnetic resonance techniques. The features of each structure are described and similarities and differences between them are discussed. The structures are combined with information from sequence homologies to produce a model of the receptor-recognition sites of EGF and TGFα, which can be tested in a site-directed mutagenesis programme. The model assists in explaining previous observations of sequence-activity relationships. The TGFα and EGF structures also serve as models for homologous modules in other extracellular proteins. |
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