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http://purl.uniprot.org/citations/22153499http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22153499http://www.w3.org/2000/01/rdf-schema#comment"The hematopoietic colony stimulating factor-1 receptor (CSF-1R or FMS) is essential for the cellular repertoire of the mammalian immune system. Here, we report a structural and mechanistic consensus for the assembly of human and mouse CSF-1:CSF-1R complexes. The EM structure of the complete extracellular assembly of the human CSF-1:CSF-1R complex reveals how receptor dimerization by CSF-1 invokes a ternary complex featuring extensive homotypic receptor contacts and striking structural plasticity at the extremities of the complex. Studies by small-angle X-ray scattering of unliganded hCSF-1R point to large domain rearrangements upon CSF-1 binding, and provide structural evidence for the relevance of receptor predimerization at the cell surface. Comparative structural and binding studies aiming to dissect the assembly principles of human and mouse CSF-1R complexes, including a quantification of the CSF-1/CSF-1R species cross-reactivity, show that bivalent cytokine binding to receptor coupled to ensuing receptor-receptor interactions are common denominators in extracellular complex formation."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2011.10.012"xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Desfosses A."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Van Craenenbroeck K."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Savvides S.N."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Svergun D.I."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Gutsche I."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Verstraete K."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Brooks B.R."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Elegheert J."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Vergauwen B."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Shkumatov A.V."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/author"Bracke N."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/pages"1762-1772"xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/title"Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles."xsd:string
http://purl.uniprot.org/citations/22153499http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/22153499http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22153499
http://purl.uniprot.org/citations/22153499http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22153499
http://purl.uniprot.org/uniprot/P09603#attribution-BE2DC90FAEAA5E5171BA2B5B6907F915http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22153499
http://purl.uniprot.org/uniprot/#_A0A494BA23-mappedCitation-22153499http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22153499
http://purl.uniprot.org/uniprot/#_A0A494BBK8-mappedCitation-22153499http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22153499