Structure function relationships in EGF, TGF-alpha and IGFI.

I D Campbell; R M Cooke

doi:10.1242/jcs.1990.supplement_13.2

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Structure function relationships in EGF, TGF-alpha and IGFI.

I D Campbell·R M Cooke

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Abstract

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.

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Animals Cell Line Epidermal Growth Factor ErbB Receptors Insulin-Like Growth Factor I Magnetic Resonance Spectroscopy Receptors, Cell Surface Receptors, Somatomedin Structure-Activity Relationship Transforming Growth Factor alpha Comparative Study Journal Article Research Support, Non-U.S. Gov't

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I D Campbell, R M Cooke. 1990. Structure function relationships in EGF, TGF-alpha and IGFI.. https://doi.org/10.1242/jcs.1990.supplement_13.2

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