Structure of the Extracellular Region of HER3 Reveals an Interdomain Tether

  title={Structure of the Extracellular Region of HER3 Reveals an Interdomain Tether},
  author={Hyun-soo Cho and Daniel J. Leahy},
  pages={1330 - 1333}
We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family. The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor. The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both… 
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A structural perspective on the regulation of the epidermal growth factor receptor.
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The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
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The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*
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Dimerization of the Extracellular Domain of the Receptor for Epidermal Growth Factor Containing the Membrane-spanning Segment in Response to Treatment with Epidermal Growth Factor*
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Two EGF molecules contribute additively to stabilization of the EGFR dimer
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