title: Putting together structures of epidermal growth factor receptors.
abstract: Numerous crystal structures have been reported for the isolated extracellular region and tyrosine kinase domain of the epidermal growth factor receptor (EGFR) and its relatives, in different states of activation and bound to a variety of inhibitors used in cancer therapy. The next challenge is to put these structures together accurately in functional models of the intact receptor in its membrane environment. The intact EGFR has been studied using electron microscopy, chemical biology methods, biochemically, and computationally. The distinct approaches yield different impressions about the structural modes of communication between extracellular and intracellular regions. They highlight possible differences between ligands, and also underline the need to understand how the receptor interacts with the membrane itself.
authors.affiliation: Graduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, United States; Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, United States.
authors.forename: Nicholas J
authors.initials: NJ
authors.lastname: Bessman
authors.affiliation: Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, United States.
authors.forename: Daniel M
authors.initials: DM
authors.lastname: Freed
authors.affiliation: Graduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, United States; Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, United States. Electronic address: mlemmon@mail.med.upenn.edu.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Lemmon
mesh_terms: D004815:Epidermal Growth Factor / Q000737:chemistry; D066246:ErbB Receptors / Q000737:chemistry*; D006801:Humans; D008024:Ligands; D008854:Microscopy, Electron; D055503:Protein Multimerization
chemical_list: D008024:Ligands; D004815:Epidermal Growth Factor; D066246:ErbB Receptors