Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor
By C. Wiesmann, M. Ultsch, S. Bass, A. D. Vos. 1999
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Citations in the corpus
- Scaffolding protein functional sites using deep learning (2022, methodology): “The nerve growth factor receptor TrkA dimerizes upon ligand binding (39), and starting from the TrkA-NGF crystal structure we positioned helical segments derived from two copies of a previously designed TrkA binding protein (4) and used hallucination followed by inpainting (Materials and Methods)…”
- Neurotrophins: roles in neuronal development and function. (2001, background): “…short polypeptide sequence was not localized in the three-dimensional structure of the NGF-TrkA ligand binding domain complex, the organization of the interface between the two proteins is compatible with the possibility that these residues may directly participate in binding (Wiesmann et al 1999).”
- Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors. (2007, background): “Of the five TrkA domains, only the C-terminal Ig-C2 domain interacts with NGF in the complex structure, as originally seen in the truncated complex structure (Wiesmann et al., 1999).”
- GDNF, NGF and BDNF as therapeutic options for neurodegeneration. (2013, background): “For each Trk receptor, only the domain closest to the membrane (called d5 or Ig2) is required to bind to its neurotrophin ligand (Wiesmann et al., 1999; Banfield et al., 2001; Naylor et al., 2002).”
- Neurotrophins: key regulators of cell fate and cell shape in the vertebrate nervous system. (2000, unknown): “(Wiesmann et al. 1999).”
- An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. (2003, background): “J. Biol. binding domain of the TrkA receptor.”