The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors

Thomas P.J. Garrett, Neil M. McKern, Meizhen Lou, Thomas C. Elleman, Timothy E. Adams, George O. Lovrecz, Michael Kofler, Robert N. Jorissen, Edouard C. Nice, Antony W. Burgess, Colin W. Ward

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421 Citations (Scopus)

Abstract

ErbB2 does not bind ligand, yet appears to be the major signaling partner for other ErbB receptors by forming heteromeric complexes with ErbB1, ErbB3, or ErbB4. The crystal structure of residues 1-509 of ErbB2 at 2.5 Å resolution reveals an activated conformation similar to that of the EGFR when complexed with ligand and very different from that seen in the unactivated forms of ErbB3 or EGFR. The structure explains the inability of ErbB2 to bind known ligands and suggests why ErbB2 fails to form homodimers. Together, the data suggest a model in which ErbB2 is already in the activated conformation and ready to interact with other ligand-activated ErbB receptors.

Original languageEnglish
Pages (from-to)495-505
Number of pages11
JournalMolecular Cell
Volume11
Issue number2
DOIs
Publication statusPublished - 1 Feb 2003

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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