EGF-like domain QuickView - Correlation Engine

Description:: A sequence of about thirty to forty amino-acid residues long found in thesequence of epidermal growth factor (EGF) has been shown to bepresent, in a more or less conserved form, in a large number of other, mostlyanimal proteins. EGF is a polypeptide of about 50 amino acids with threeinternal disulfide bridges. It first binds with high affinity to specificcell-surface receptors and then induces their dimerization, which is essentialfor activating the tyrosine kinase in the receptor cytoplasmic domain,initiating a signal transduction that results in DNA synthesis and cellproliferation.A common feature of all EGF-like domains is that they are found in theextracellular domain of membrane-bound proteins or in proteins known to besecreted (exception: prostaglandin G/H synthase). The EGF-like domain includessix cysteine residues which have been shown to be involved in disulfide bonds.The structure of several EGF-like domains has been solved. The fold consistsof two-stranded beta-sheet followed by a loop to a C-terminal shorttwo-stranded sheet.