http://purl.uniprot.org/citations/21134643 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21134643 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21134643 | http://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/21134643 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2010.09.016"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2010.09.016"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "McIntosh L.P."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "McIntosh L.P."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Escobar-Cabrera E."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Escobar-Cabrera E."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Ishov A.M."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Ishov A.M."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Giovinazzi S."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Giovinazzi S."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Lau D.K."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/author | "Lau D.K."xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/pages | "1642-1653"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/pages | "1642-1653"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://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/21134643 | http://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/21134643 | http://purl.uniprot.org/core/volume | "18"xsd:string |
http://purl.uniprot.org/citations/21134643 | http://purl.uniprot.org/core/volume | "18"xsd:string |