RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/28392261http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28392261http://www.w3.org/2000/01/rdf-schema#comment"The N-end rule pathway controls the half-life of proteins based on their N-terminal residue. Positively charged type 1 N-degrons are recognized by a negatively charged pocket on the Zn finger named the UBR box. Here, we show that the UBR box is rigid, but bound water molecules in the pocket provide the structural plasticity required to bind different positively charged amino acids. Ultra-high-resolution crystal structures of arginine, histidine, and methylated arginine reveal that water molecules mediate the binding of N-degron peptides. Using a high-throughput binding assay and isothermal titration calorimetry, we demonstrate that the UBR box is able to bind methylated arginine and lysine peptides with high affinity and measure the preference for hydrophobic residues in the second position in the N-degron peptide. Finally, we show that the V122L mutation present in Johanson-Blizzard syndrome patients changes the specificity for the second position due to occlusion of the secondary pocket."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2017.03.004"xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/author"Gehring K."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/author"Kozlov G."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/author"Matta-Camacho E."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/author"Cho C."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/author"Munoz-Escobar J."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/pages"719-729.e3"xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/title"Bound Waters Mediate Binding of Diverse Substrates to a Ubiquitin Ligase."xsd:string
http://purl.uniprot.org/citations/28392261http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/28392261http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28392261
http://purl.uniprot.org/citations/28392261http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28392261
http://purl.uniprot.org/uniprot/#_Q8IWV7-mappedCitation-28392261http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28392261
http://purl.uniprot.org/uniprot/#_Q8IWV8-mappedCitation-28392261http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28392261
http://purl.uniprot.org/uniprot/Q8IWV7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28392261
http://purl.uniprot.org/uniprot/Q8IWV8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28392261