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http://purl.uniprot.org/citations/11524679http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11524679http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11524679http://www.w3.org/2000/01/rdf-schema#comment"The pathogenesis of transmissible encephalopathies is associated with the conversion of the cellular prion protein, PrP(C), into a conformationally altered oligomeric form, PrP(Sc). Here we report the crystal structure of the human prion protein in dimer form at 2 A resolution. The dimer results from the three-dimensional swapping of the C-terminal helix 3 and rearrangement of the disulfide bond. An interchain two-stranded antiparallel beta-sheet is formed at the dimer interface by residues that are located in helix 2 in the monomeric NMR structures. Familial prion disease mutations map to the regions directly involved in helix swapping. This crystal structure suggests that oligomerization through 3D domain-swapping may constitute an important step on the pathway of the PrP(C) --> PrP(Sc) conversion."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.org/dc/terms/identifier"doi:10.1038/nsb0901-770"xsd:string
http://purl.uniprot.org/citations/11524679http://purl.org/dc/terms/identifier"doi:10.1038/nsb0901-770"xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Yee V.C."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Yee V.C."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Surewicz W.K."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Surewicz W.K."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Morillas M."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Morillas M."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Malone M."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Malone M."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Swietnicki W."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Swietnicki W."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Knaus K.J."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/author"Knaus K.J."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/pages"770-774"xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/pages"770-774"xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/title"Crystal structure of the human prion protein reveals a mechanism for oligomerization."xsd:string
http://purl.uniprot.org/citations/11524679http://purl.uniprot.org/core/title"Crystal structure of the human prion protein reveals a mechanism for oligomerization."xsd:string