title: Regulation of the catalytic activity of the EGF receptor.
abstract: The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase involved in cell growth that is often misregulated in cancer. Several recent studies highlight the unique structural mechanisms involved in its regulation. Some elucidate the important role that the juxtamembrane segment and the transmembrane helix play in stabilizing the activating asymmetric kinase dimer, and suggest that its activation mechanism is likely to be conserved among the other human EGFR-related receptors. Other studies provide new explanations for two long observed, but poorly understood phenomena, the apparent heterogeneity in ligand binding and the formation of ligand-independent dimers. New insights into the allosteric mechanisms utilized by intracellular regulators of EGFR provide hope that allosteric sites could be used as targets for drug development.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
authors.forename: Nicholas F
authors.initials: NF
authors.lastname: Endres
authors.forename: Kate
authors.initials: K
authors.lastname: Engel
authors.forename: Rahul
authors.initials: R
authors.lastname: Das
authors.forename: Erika
authors.initials: E
authors.lastname: Kovacs
authors.forename: John
authors.initials: J
authors.lastname: Kuriyan
mesh_terms: D000494:Allosteric Regulation; D000495:Allosteric Site; D002384:Catalysis; D002462:Cell Membrane / Q000378:metabolism; D019281:Dimerization; D004815:Epidermal Growth Factor / Q000378:metabolism; D066246:ErbB Receptors / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D008024:Ligands; D004815:Epidermal Growth Factor; D066246:ErbB Receptors