Abstract
Epidermal growth factor (EGF) is a small peptide growth factor which mediates its response by a membrane glcoprotein denoted as the EGF-receptor,(reviewed in 1–2). Following the purification of the EGF-receptor,3 and its partial sequencing,4 the complete primary structure of the EGF-receptor was deduced from nucleotide sequence of cDNA clones.5 The mature receptor is composed of 1,186 amino acid residues that are preceded at the NH2-terminal end by a signal peptide of 24 hydrophobic amino acids. The signal peptide is cleaved after insertion of the nascent receptor into the membrane of the endoplasmic reticulum. Cotranslationally, the receptor is glycosylated and transported through the Golgi apparatus to the plasma membrane. The mature receptor is composed of three major structural elements. An extracellular EGF-binding domain composed of 621 amino acid residues, anchored to the plasma membrane by a single transmembrane region of 23 hydrophobic amino acids. The transmembrane region is followed by a sequence of mostly basic residues; a feature common to many membrane proteins.
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Schlessinger, J. (1988). Regulation of Cell Growth and Transformation by the Epidermal Growth Factor Receptor. In: Kudlow, J.E., MacLennan, D.H., Bernstein, A., Gotlieb, A.I. (eds) Biology of Growth Factors. Advances in Experimental Medicine and Biology, vol 234. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1980-2_6
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DOI: https://doi.org/10.1007/978-1-4757-1980-2_6
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