title: Investigating extracellular in situ EGFR structure and conformational changes using FRET microscopy.
abstract: The crystallographic structures of functional fragments of ErbBs have provided excellent insights into the geometry of growth factor binding and receptor dimerization. By placing together receptor fragments to build structural models of entire receptors, we expect to understand how these enzymes are allosterically regulated; however, several predictions from these models are inconsistent with experimental evidence from cells. The opening of this gap underlines the need to investigate intact ErbBs by combining cellular and structural studies into a full picture.
authors.affiliation: Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, Oxon OX11 0QX, UK.
authors.forename: Selene K
authors.initials: SK
authors.lastname: Roberts
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Tynan
authors.forename: Martyn
authors.initials: M
authors.lastname: Winn
authors.forename: Marisa L
authors.initials: ML
authors.lastname: Martin-Fernandez
mesh_terms: D004815:Epidermal Growth Factor / Q000378:metabolism; D066246:ErbB Receptors / Q000737:chemistry* / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
chemical_list: D004815:Epidermal Growth Factor; C512478:EGFR protein, human; D066246:ErbB Receptors