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http://purl.uniprot.org/citations/19220853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19220853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19220853http://www.w3.org/2000/01/rdf-schema#comment"Plant pathogenesis-related (PR) proteins of class 10 are the only group among the 17 PR protein families that are intracellular and cytosolic. Sequence conservation and the wide distribution of PR-10 proteins throughout the plant kingdom are an indication of an indispensable function in plants, but their true biological role remains obscure. Crystal and solution structures for several homologues have shown a similar overall fold with a vast internal cavity which, together with structural similarities to the steroidogenic acute regulatory protein-related lipid transfer domain and cytokinin-specific binding proteins, strongly indicate a ligand-binding role for the PR-10 proteins. This article describes the structure of a complex between a classic PR-10 protein [Lupinus luteus (yellow lupine) PR-10 protein of subclass 2, LlPR-10.2B] and N,N'-diphenylurea, a synthetic cytokinin. Synthetic cytokinins have been shown in various bioassays to exhibit activity similar to that of natural cytokinins. The present 1.95 A resolution crystallographic model reveals four N,N'-diphenylurea molecules in the hydrophobic cavity of the protein and a degree of conformational changes accompanying ligand binding. The structural adaptability of LlPR-10.2B and its ability to bind different cytokinins suggest that this protein, and perhaps other PR-10 proteins as well, can act as a reservoir of cytokinin molecules in the aqueous environment of a plant cell."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2009.06892.x"xsd:string
http://purl.uniprot.org/citations/19220853http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2009.06892.x"xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Jasinski M."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Jasinski M."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Bujacz A."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Bujacz A."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Bujacz G."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Bujacz G."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Jaskolski M."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Jaskolski M."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Otlewski J."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Otlewski J."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Kachlicki P."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Kachlicki P."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Sikorski M.M."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Sikorski M.M."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Fernandes H."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Fernandes H."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Jelen F."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/author"Jelen F."xsd:string
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19220853http://purl.uniprot.org/core/date"2009"xsd:gYear