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http://purl.uniprot.org/citations/19731378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19731378http://www.w3.org/2000/01/rdf-schema#comment"The covalent attachment of different types of poly-ubiquitin chains signal different outcomes for the proteins so targeted. For example, a protein modified with Lys-48-linked poly-ubiquitin chains is targeted for proteasomal degradation, whereas Lys-63-linked chains encode nondegradative signals. The structural features that enable these different types of chains to encode different signals have not yet been fully elucidated. We report here the X-ray crystal structures of Lys-63-linked tri- and di-ubiquitin at resolutions of 2.3 and 1.9 A, respectively. The tri- and di-ubiquitin species adopt essentially identical structures. In both instances, the ubiquitin chain assumes a highly extended conformation with a left-handed helical twist; the helical chain contains four ubiquitin monomers per turn and has a repeat length of approximately 110 A. Interestingly, Lys-48 ubiquitin chains also adopt a left-handed helical structure with a similar repeat length. However, the Lys-63 architecture is much more open than that of Lys-48 chains and exposes much more of the ubiquitin surface for potential recognition events. These new crystal structures are consistent with the results of solution studies of Lys-63 chain conformation, and reveal the structural basis for differential recognition of Lys-63 versus Lys-48 chains."xsd:string
http://purl.uniprot.org/citations/19731378http://purl.org/dc/terms/identifier"doi:10.1002/prot.22568"xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/author"Weeks S.D."xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/author"Grasty K.C."xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/author"Hernandez-Cuebas L."xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/author"Loll P.J."xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/name"Proteins"xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/pages"753-759"xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/title"Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture."xsd:string
http://purl.uniprot.org/citations/19731378http://purl.uniprot.org/core/volume"77"xsd:string
http://purl.uniprot.org/citations/19731378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19731378
http://purl.uniprot.org/citations/19731378http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19731378
http://purl.uniprot.org/uniprot/#_P0CG48-mappedCitation-19731378http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19731378
http://purl.uniprot.org/uniprot/P0CG48http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19731378