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http://purl.uniprot.org/citations/10490030http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10490030http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10490030http://www.w3.org/2000/01/rdf-schema#comment"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. 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 (TrkA-d5 domain) is necessary and sufficient for NGF binding. Here we present the crystal structure of human NGF in complex with human TrkA-d5 at 2.2 A resolution. The ligand-receptor interface consists of two patches of similar size. One patch involves the central beta-sheet that forms the core of the homodimeric NGF molecule and the loops at the carboxy-terminal pole of TrkA-d5. The second patch comprises the amino-terminal residues of NGF, which adopt a helical conformation upon complex formation, packing against the 'ABED' sheet of TrkA-d5. The structure is consistent with results from mutagenesis experiments for all neurotrophins, and indicates that the first patch may constitute a conserved binding motif for all family members, whereas the second patch is specific for the interaction between NGF and TrkA."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.org/dc/terms/identifier"doi:10.1038/43705"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.org/dc/terms/identifier"doi:10.1038/43705"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"Wiesmann C."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"Wiesmann C."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"de Vos A.M."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"de Vos A.M."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"Bass S.H."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"Bass S.H."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"Ultsch M.H."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/author"Ultsch M.H."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/pages"184-188"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/pages"184-188"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/title"Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/title"Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor."xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/volume"401"xsd:string
http://purl.uniprot.org/citations/10490030http://purl.uniprot.org/core/volume"401"xsd:string
http://purl.uniprot.org/citations/10490030http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10490030
http://purl.uniprot.org/citations/10490030http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10490030