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http://purl.uniprot.org/citations/21134643http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21134643http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21134643http://www.w3.org/2000/01/rdf-schema#comment"DAXX is a scaffold protein with diverse roles including transcription and cell cycle regulation. Using NMR spectroscopy, we demonstrate that the C-terminal half of DAXX is intrinsically disordered, whereas a folded domain is present near its N terminus. This domain forms a left-handed four-helix bundle (H1, H2, H4, H5). However, due to a crossover helix (H3), this topology differs from that of the Sin3 PAH domain, which to date has been used as a model for DAXX. The N-terminal residues of the tumor suppressor Rassf1C fold into an amphipathic α helix upon binding this DAXX domain via a shallow cleft along the flexible helices H2 and H5 (K(D) ∼60 μM). Based on a proposed DAXX recognition motif as hydrophobic residues preceded by negatively charged groups, we found that peptide models of p53 and Mdm2 also bound the helical bundle. These data provide a structural foundation for understanding the diverse functions of DAXX."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2010.09.016"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2010.09.016"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"McIntosh L.P."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"McIntosh L.P."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Escobar-Cabrera E."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Escobar-Cabrera E."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Ishov A.M."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Ishov A.M."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Giovinazzi S."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Giovinazzi S."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Lau D.K."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/author"Lau D.K."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/pages"1642-1653"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/pages"1642-1653"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/title"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/title"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C."xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/21134643http://purl.uniprot.org/core/volume"18"xsd:string