title: The EGF receptor Hokey-Cokey.
abstract: In cancer, the epidermal growth factor (EGF) receptor (EGFR) can be activated by mutations that disrupt the inactive conformation and allow the active conformation to predominate. Structural studies have elucidated the molecular events that lead to EGFR activation and shown that small-molecule anti-EGFR drugs can bind to either the inactive or the active conformation of the kinase domain. In this issue of Cancer Cell, Yun et al. present 12 crystal structures of the wild-type or mutant forms of the EGFR kinase domain bound to four different ligands. This study will prove invaluable to those developing novel anti-EGFR drugs.
authors.affiliation: The Institute of Cancer Research, Gene and Oncogene Targeting Team, Cancer Research UK Centre for Cancer Therapeutics, Sutton, Surrey SM2 5NG, UK.
authors.forename: Dan
authors.initials: D
authors.lastname: Niculescu-Duvaz
authors.forename: Steven
authors.initials: S
authors.lastname: Whittaker
authors.forename: Caroline
authors.initials: C
authors.lastname: Springer
authors.forename: Richard
authors.initials: R
authors.lastname: Marais
mesh_terms: D000970:Antineoplastic Agents / Q000737:chemistry*; D004789:Enzyme Activation; D066246:ErbB Receptors / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics; D000077156:Gefitinib; D006801:Humans; D000077341:Lapatinib; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011687:Purines / Q000737:chemistry; D011799:Quinazolines / Q000737:chemistry; D019311:Staurosporine / Q000031:analogs & derivatives / Q000737:chemistry
chemical_list: C519151:AFN941; D000970:Antineoplastic Agents; D011687:Purines; D011799:Quinazolines; D000077341:Lapatinib; D066246:ErbB Receptors; C489254:AEE 788; D019311:Staurosporine; D000077156:Gefitinib