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http://purl.uniprot.org/citations/33647291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33647291http://www.w3.org/2000/01/rdf-schema#comment"Retinoic acid receptors (RARs) and retinoid X receptors (RXRs) form heterodimers that activate target gene transcription by recruiting co-activator complexes in response to ligand binding. The nuclear receptor (NR) co-activator TIF2 mediates this recruitment by interacting with the ligand-binding domain (LBD) of NRs trough the nuclear receptor interaction domain (TIF2NRID) containing three highly conserved α-helical LxxLL motifs (NR-boxes). The precise binding mode of this domain to RXR/RAR is not clear due to the disordered nature of TIF2. Here we present the structural characterization of TIF2NRID by integrating several experimental (NMR, SAXS, Far-UV CD, SEC-MALS) and computational data. Collectively, the data are in agreement with a largely disordered protein with partially structured regions, including the NR-boxes and their flanking regions, which are evolutionary conserved. NMR and X-ray crystallographic data on TIF2NRID in complex with RXR/RAR reveal a multisite binding of the three NR-boxes as well as an active role of their flanking regions in the interaction."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2021.166899"xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Allemand F."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Schubert M."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Sibille N."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Bourguet W."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Bernado P."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Carvalho J.E."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"le Maire A."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Germain P."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Senicourt L."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/author"Guee L."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/pages"166899"xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/title"Structural Insights into the Interaction of the Intrinsically Disordered Co-activator TIF2 with Retinoic Acid Receptor Heterodimer (RXR/RAR)."xsd:string
http://purl.uniprot.org/citations/33647291http://purl.uniprot.org/core/volume"433"xsd:string
http://purl.uniprot.org/citations/33647291http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33647291
http://purl.uniprot.org/citations/33647291http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33647291
http://purl.uniprot.org/uniprot/#_P10276-mappedCitation-33647291http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33647291
http://purl.uniprot.org/uniprot/#_Q15596-mappedCitation-33647291http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33647291
http://purl.uniprot.org/uniprot/#_A0A0B6XJZ8-mappedCitation-33647291http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33647291
http://purl.uniprot.org/uniprot/#_A3FFT2-mappedCitation-33647291http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33647291
http://purl.uniprot.org/uniprot/#_A2AJP1-mappedCitation-33647291http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33647291