InterPro domain: IPR000742

A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF) has been shown [ 1 , 2 , 3 , 4 ] to be present, in a more or less conserved form, in a large number of other, mostly animal, proteins. EGF is a polypeptide of about 50 amino acids with three internal disulfide bridges. It first binds with high affinity to specific cell-surface receptors and then induces their dimerization, which is essential for activating the tyrosine kinase in the receptor cytoplasmic domain, initiating a signal transduction that results in DNA synthesis and cell proliferation.

A common feature of all EGF-like domains is that they are found in the extracellular domain of membrane-bound proteins or in proteins known to besecreted (exception: prostaglandin G/H synthase). The EGF-like domain includes six cysteine residues which have been shown to be involved in disulfide bonds. The structure of several EGF-like domains has been solved. The fold consists of two-stranded beta-sheet followed by a loop to a C-terminal shorttwo-stranded sheet.

1. The many faces of epidermal growth factor repeats. New Biol. 2, 410-9
2. Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc. Natl. Acad. Sci. U.S.A. 81, 7363-7
3. Computer-based characterization of epidermal growth factor precursor. Nature 307, 558-60
4. Structure and function of epidermal growth factor-like regions in proteins. FEBS Lett. 231, 1-4