| http://purl.uniprot.org/citations/32257053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32257053 | http://www.w3.org/2000/01/rdf-schema#comment | "The density regulated protein (DENR) forms a stable heterodimer with malignant T-cell-amplified sequence 1 (MCT-1). DENR-MCT-1 heterodimer then participates in regulation of non-canonical translation initiation and ribosomal recycling. The N-terminal domain of DENR interacts with MCT-1 and carries a classical tetrahedral zinc ion-binding site, which is crucial for the dimerization. DENR-MCT-1 binds the small (40S) ribosomal subunit through interactions between MCT-1 and helix h24 of the 18S rRNA, and through interactions between the C-terminal domain of DENR and helix h44 of the 18S rRNA. This later interaction occurs in the vicinity of the P site that is also the binding site for canonical translation initiation factor eIF1, which plays the key role in initiation codon selection and scanning. Sequence homology modeling and a low-resolution crystal structure of the DENR-MCT-1 complex with the human 40S subunit suggests that the C-terminal domain of DENR and eIF1 adopt a similar fold. Here we present the crystal structure of the C-terminal domain of DENR determined at 1.74 Å resolution, which confirms its resemblance to eIF1 and advances our understanding of the mechanism by which DENR-MCT-1 regulates non-canonical translation initiation and ribosomal recycling."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.csbj.2020.03.009"xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/author | "Steitz T.A."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/author | "Wang J."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/author | "De S."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/author | "Lomakin I.B."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/author | "Borkar A.N."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/name | "Comput Struct Biotechnol J"xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/pages | "696-704"xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/title | "Crystal structure of the C-terminal domain of DENR."xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://purl.uniprot.org/core/volume | "18"xsd:string |
| http://purl.uniprot.org/citations/32257053 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32257053 |
| http://purl.uniprot.org/citations/32257053 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/32257053 |
| http://purl.uniprot.org/uniprot/#_O43583-mappedCitation-32257053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32257053 |
| http://purl.uniprot.org/uniprot/O43583 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32257053 |