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http://purl.uniprot.org/citations/19073700http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19073700http://www.w3.org/2000/01/rdf-schema#comment"Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by enzymatically depurinating a specific adenine residue at the sarcin-ricin loop of the 28S rRNA, which thereby prevents the binding of elongation factors to the GTPase activation centre of the ribosome. Here, we present the 2.2 A crystal structure of trichosanthin (TCS) complexed to the peptide SDDDMGFGLFD, which corresponds to the conserved C-terminal elongation factor binding domain of the ribosomal P protein. The N-terminal region of this peptide interacts with Lys173, Arg174 and Lys177 in TCS, while the C-terminal region is inserted into a hydrophobic pocket. The interaction with the P protein contributes to the ribosome-inactivating activity of TCS. This 11-mer C-terminal P peptide can be docked with selected important plant and bacterial RIPs, indicating that a similar interaction may also occur with other RIPs."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkn922"xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Shaw P.C."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Zhu G."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Au S.W."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Wong K.B."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Mak A.N."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Too P.H."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Wong Y.T."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Tung C.K."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/author"Ma M.K."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/name"Nucleic Acids Res"xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/pages"602-610"xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/title"The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome."xsd:string
http://purl.uniprot.org/citations/19073700http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/19073700http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19073700
http://purl.uniprot.org/citations/19073700http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19073700
http://purl.uniprot.org/uniprot/#_P09989-mappedCitation-19073700http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19073700
http://purl.uniprot.org/uniprot/#_P05387-mappedCitation-19073700http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19073700
http://purl.uniprot.org/uniprot/P05387http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19073700
http://purl.uniprot.org/uniprot/P09989http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19073700