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http://purl.uniprot.org/citations/17646174http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17646174http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17646174http://www.w3.org/2000/01/rdf-schema#comment"beta(2)-Microglobulin (beta2-m), a light chain of the major histocompatibility complex class I, forms amyloid fibrils in patients undergoing long-term haemodialysis, causing dialysis-related amyloidosis. Based on a comparison of the X-ray structure obtained at pH 5.7 and that of beta2-m in the histocompatibility complex, it has been proposed that the continuous D-strand observed in the crystal structure at pH 5.7 increases the propensity of beta2-m to self-associate via edge-to-edge interactions, thus initiating the formation of fibrils. To obtain further insight into the mechanism by which amyloid fibrils form, we determined the crystal structure of beta2-m at pH 7.0 at a resolution of up to 1.13 A. The crystal structure at pH 7.0 was basically the same as that at pH 5.6, suggesting that the conversion of the beta-bulge in strand D into a contiguous beta-strand is not unique to the crystals formed under slightly acidic conditions. In other words, although the formation of beta2-m fibrils was enhanced under acidic conditions, it remains unknown if it is related to the increased propensity for the disappearance of the beta-bulge in strand D. We consider that the enhanced fibrillation is more directly coupled with the decreased stability leading to the increased propensity of exposing amyloidogenic regions."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvm148"xsd:string
http://purl.uniprot.org/citations/17646174http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvm148"xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Goto Y."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Goto Y."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Nakagawa A."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Nakagawa A."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Iwata K."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Iwata K."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Sakurai K."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Sakurai K."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Matsuura T."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/author"Matsuura T."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/pages"413-419"xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/pages"413-419"xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/title"High-resolution crystal structure of beta2-microglobulin formed at pH 7.0."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/title"High-resolution crystal structure of beta2-microglobulin formed at pH 7.0."xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/volume"142"xsd:string
http://purl.uniprot.org/citations/17646174http://purl.uniprot.org/core/volume"142"xsd:string