Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor

@article{Wiesmann1999CrystalSO,
  title={Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor},
  author={C. Wiesmann and M. Ultsch and S. Bass and A. Vos},
  journal={Nature},
  year={1999},
  volume={401},
  pages={184-188}
}
  • C. Wiesmann, M. Ultsch, +1 author A. Vos
  • Published 1999
  • Biology, Medicine
  • Nature
    • Nerve growth factor (NGF) is involved in a variety of processes involving signalling, such as cell differentiation and survival, growth cessation and apoptosis of neurons. These events are mediated by NGF as a result of binding to its two cell-surface receptors, TrkA and p75 (ref. 2). TrkA is a receptor with tyrosine kinase activity that forms a high-affinity binding site for NGF. Of the five domains comprising its extracellular portion, the immunoglobulin-like domain proximal to the membrane… CONTINUE READING
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    347 Citations
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    TrkA Amino Acids Controlling Specificity for Nerve Growth Factor*
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    Structural Basis of the Transmembrane Domain Dimerization in the Activation Mechanism of TrkA by NGF
    The Mechanism of NGF Signaling Suggested by the p75 and TrkA Receptor Complexes
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