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http://purl.uniprot.org/citations/12173935http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12173935http://www.w3.org/2000/01/rdf-schema#comment"Angiogenin and ribonuclease A share 33% sequence identity but have distinct functions. Angiogenin is a potent inducer of angiogenesis that is only weakly ribonucleolytic, whereas ribonuclease A is a robust ribonuclease that is not angiogenic. A chimera ("ARH-I"), in which angiogenin residues 58-70 are replaced with residues 59-73 of ribonuclease A, has intermediate ribonucleolytic potency and no angiogenic activity. Here we report a crystal structure of ARH-I that reveals the molecular basis for these characteristics. The ribonuclease A-derived (guest) segment adopts a structure largely similar to that in ribonuclease A, and successfully converts this region from a cell-binding site to a purine-binding site. At the same time, its presence causes complex changes in the angiogenin-derived (host) portion that account for much of the increased ribonuclease activity of ARH-I. Guest-host interactions of this type probably occur more generally in protein chimeras, emphasizing the importance of direct structural information for understanding the functional behavior of such molecules."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.org/dc/terms/identifier"doi:10.1021/bi026151r"xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/author"Acharya K.R."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/author"Holloway D.E."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/author"Shapiro R."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/author"Hares M.C."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/author"Leonidas D.D."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/pages"10482-10489"xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/title"Guest-host crosstalk in an angiogenin-RNase A chimeric protein."xsd:string
http://purl.uniprot.org/citations/12173935http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/12173935http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12173935
http://purl.uniprot.org/citations/12173935http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12173935
http://purl.uniprot.org/uniprot/#_P61823-mappedCitation-12173935http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12173935
http://purl.uniprot.org/uniprot/#_P03950-mappedCitation-12173935http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12173935
http://purl.uniprot.org/uniprot/P03950http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12173935
http://purl.uniprot.org/uniprot/P61823http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12173935