Abstract
Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be indispensable for EGF binding to its receptor are involved in the interface between the two EGF molecules, suggesting a crucial role of EGF dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure of mouse EGF determined at pH 2.0, but structural comparisons between different models have revealed new detailed features and properties of the EGF structure.
Highlights
Human epidermal growth factor1 is a polypeptide of 53 amino acids with three internal disulfide bridges
Except the two terminal segments, most main-chains in both Human epidermal growth factor (hEGF) molecules have well defined electron densities when contoured at 1 level (Fig. 1)
The crystal structure of hEGF determined at near physiological pH shares the main features of the NMR structure of mouse EGF (mEGF) determined at pH 2.0, but structural comparisons between different models revealed further details of the Epidermal growth factor (EGF) structure
Summary
Epidermal growth factor (EGF) is a typical growthstimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. EGF was found to exist predominantly as a monomeric species in solution, and based on analyses of binding of EGF to the extracellular domain of its receptor and of the resulting dimerization of the receptor, some models have been proposed for EGF-induced dimerization of receptors [3]. All these models have yet to be verified by structural studies, the most important of which is the structural determination of the complex of EGF with its receptor. Analyses of the crystal structure and comparisons with NMR solution structures have revealed new details of the features and properties of the hEGF structure
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
