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- W2097639959 abstract "Motifs in ligand-binding domains of the neurotrophin (NTR) and lymphotoxin (TNFR-I) receptors define a family of receptors that mediates programmed cell death. We have explored relationships of architecture and function in this family through a molecular model of NTR, also called p75NGFR or LANR. Modeling by homology took advantage of four modular subdomains in the crystal structure of TNFR-1 that also occur in NTR. Hypothetical complexes between the model and a ligand structure (for nerve growth factor, NGF) were then examined using docking software. NTR appears to bind in the dimer interface of NGF, making two sets of contacts. NTR subdomains III and IV provide the ligand-contact surfaces, in contrast to TNFR, in which subdomains II and III contact TNF-β. NTR subdomain II appears to have been evolutionarily modified, potentially contributing to an interface between receptor subunits. These and other specific predictions of the model will require experimental confirmation." @default.
- W2097639959 created "2016-06-24" @default.
- W2097639959 creator A5053276616 @default.
- W2097639959 creator A5059465522 @default.
- W2097639959 date "1995-09-01" @default.
- W2097639959 modified "2023-10-10" @default.
- W2097639959 title "Modeled structure of the 75-kDa neurotrophin receptor" @default.
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- W2097639959 doi "https://doi.org/10.1002/pro.5560040905" @default.
- W2097639959 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2143228" @default.
- W2097639959 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8528068" @default.
- W2097639959 hasPublicationYear "1995" @default.
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