Inhibition of ErbB3 by a monoclonal antibody that locks the extracellular domain in an inactive configuration.

@article{Lee2015InhibitionOE,
  title={Inhibition of ErbB3 by a monoclonal antibody that locks the extracellular domain in an inactive configuration.},
  author={SangWon Lee and Etienne B Greenlee and Joseph R Amick and Gwenda F. Ligon and Jay S Lillquist and Edward J Natoli and Yaron Hadari and Diego Beltran Alvarado and Joseph Schlessinger},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2015},
  volume={112 43},
  pages={13225-30}
}
ErbB3 (HER3) is a member of the EGF receptor (EGFR) family of receptor tyrosine kinases, which, unlike the other three family members, contains a pseudo kinase in place of a tyrosine kinase domain. In cancer, ErbB3 activation is driven by a ligand-dependent mechanism through the formation of heterodimers with EGFR, ErbB2, or ErbB4 or via a ligand-independent process through heterodimerization with ErbB2 overexpressed in breast tumors or other cancers. Here we describe the crystal structure of… CONTINUE READING
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