Rigidity of the extracellular part of HER2: Evidence from engineering subdomain interfaces and shared‐helix DARPin‐DARPin fusions

@article{Jost2017RigidityOT,
  title={Rigidity of the extracellular part of HER2: Evidence from engineering subdomain interfaces and shared‐helix DARPin‐DARPin fusions},
  author={C. Jost and Jakob C St{\"u}ber and A. Honegger and Y. Wu and A. Batyuk and A. Pl{\"u}ckthun},
  journal={Protein Science},
  year={2017},
  volume={26}
}
  • C. Jost, Jakob C Stüber, +3 authors A. Plückthun
  • Published 2017
  • Biology, Medicine
  • Protein Science
  • The second member of the human ErbB family of receptor tyrosine kinases, HER2/hErbB2, is regarded as an exceptional case: The four extracellular subdomains could so far only be found in one fixed overall conformation, designated “open” and resembling the ligand‐bound form of the other ErbB receptors. It thus appears to be different from the extracellular domains of the other family members that show inter‐subdomain flexibility and exist in a “tethered” form in the absence of ligand. For HER2… CONTINUE READING
    6 Citations

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