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http://purl.uniprot.org/citations/18842587http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18842587http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18842587http://www.w3.org/2000/01/rdf-schema#comment"Post-translational modification by small ubiquitin-like modifier (SUMO) proteins has been implicated in the regulation of a variety of cellular events. The functions of sumoylation are often mediated by downstream effector proteins harboring SUMO-interacting motifs (SIMs) that are composed of a hydrophobic core and a stretch of acidic residues. MBD1-containing chromatin-associated factor 1 (MCAF1), a transcription repressor, interacts with SUMO-2/3 and SUMO-1, with a preference for SUMO-2/3. We used NMR spectroscopy to solve the solution structure of the SIM of MCAF1 bound to SUMO-3. The hydrophobic core of the SIM forms a parallel beta-sheet pairing with strand beta2 of SUMO-3, whereas its C-terminal acidic stretch seems to mediate electrostatic interactions with a surface area formed by basic residues of SUMO-3. The significance of these electrostatic interactions was shown by mutations of both SUMO-3 and MCAF1. The present structural and biochemical data suggest that the acidic stretch of the SIM of MCAF1 plays an important role in the binding to SUMO-3."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m802528200"xsd:string
http://purl.uniprot.org/citations/18842587http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m802528200"xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Shirakawa M."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Shirakawa M."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Yamane T."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Yamane T."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Tochio H."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Tochio H."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Ariyoshi M."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Ariyoshi M."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Uchimura Y."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Uchimura Y."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Ikegami T."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Ikegami T."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Saitoh H."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Saitoh H."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Ikeguchi M."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Ikeguchi M."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Baba D."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Baba D."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Sekiyama N."xsd:string
http://purl.uniprot.org/citations/18842587http://purl.uniprot.org/core/author"Sekiyama N."xsd:string