Structure function relationships in EGF, TGF-alpha and IGFI.
The solution structures of the homologous growth factors hEGF and hTGF-alpha, have been determined independently from high resolution nuclear magnetic resonance (NMR) data. A model of the insulin-like growth factor structure based on insulin coordinates (Blundell et al. (1978) Proc natn. Acad. Sci. U.S.A. 75, 180-184), has also been refined using molecular dynamics simulations with NMR-determined restraints. Knowledge of these structures, together with known sequences of other homologous proteins and experiments with site-specific residue changes, allows predictions to be made about growth factor residues which might be involved in the receptor-ligand interfaces.
Campbell
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ID
Department of Biochemistry, University of Oxford, UK.
Cooke
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RM
D000818:Animals; D002460:Cell Line; D004815:Epidermal Growth Factor / Q000737:chemistry* / Q000378:metabolism; D066246:ErbB Receptors / Q000378:metabolism; D007334:Insulin-Like Growth Factor I / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011956:Receptors, Cell Surface / Q000378:metabolism; D017451:Receptors, Somatomedin; D013329:Structure-Activity Relationship; D016211:Transforming Growth Factor alpha / Q000737:chemistry* / Q000378:metabolism
D011956:Receptors, Cell Surface; D017451:Receptors, Somatomedin; D016211:Transforming Growth Factor alpha; D004815:Epidermal Growth Factor; D007334:Insulin-Like Growth Factor I; D066246:ErbB Receptors