| http://purl.uniprot.org/citations/22640416 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22640416 | http://www.w3.org/2000/01/rdf-schema#comment | "RNA helicases of the DEAD (Asp-Glu-Ala-Asp)-box family of proteins are involved in many aspects of RNA metabolism from transcription to RNA decay, but most of them have also been shown to be multifunctional. The DEAD-box helicase DDX5 of host cells has been shown to interact with the RNA-dependent RNA polymerase (NS5B) of HCV (hepatitis C virus). In the present study, we report the presence of two independent NS5B-binding sites in DDX5, one located at the N-terminus and another at the C-terminus. The N-terminal fragment of DDX5, which consists of the first 305 amino acids and shall be referred as DDX5-N, was expressed and crystallized. The crystal structure shows that domain 1 (residues 79-303) of DDX5 contains the typical features found in the structures of other DEAD-box helicases. DDX5-N also contains the highly variable NTR (N-terminal region) of unknown function and the crystal structure reveals structural elements in part of the NTR, namely residues 52-78. This region forms an extensive loop and an α-helix. From co-immunoprecipitation experiments, the NTR of DDX5-N was observed to auto-inhibit its interaction with NS5B. Interestingly, the α-helix in NTR is essential for this auto-inhibition and seems to mediate the interaction between the highly flexible 1-51 residues in NTR and the NS5B-binding site in DDX5-N. Furthermore, NMR investigations reveal that there is a direct interaction between DDX5 and NS5B in vitro."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20120001"xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Fielding B.C."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Song J."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Tan Y.J."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Dutta S."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Kotaka M."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Gupta G."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/author | "Choi Y.W."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/pages | "37-46"xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/title | "The variable N-terminal region of DDX5 contains structural elements and auto-inhibits its interaction with NS5B of hepatitis C virus."xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://purl.uniprot.org/core/volume | "446"xsd:string |
| http://purl.uniprot.org/citations/22640416 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22640416 |
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