[HTML][HTML] The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors
TPJ Garrett, NM McKern, M Lou, TC Elleman… - Molecular cell, 2003 - cell.com
TPJ Garrett, NM McKern, M Lou, TC Elleman, TE Adams, GO Lovrecz, M Kofler, RN Jorissen…
Molecular cell, 2003•cell.comErbB2 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 …
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 …
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.
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