http://purl.uniprot.org/citations/11851341 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11851341 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11851341 | http://www.w3.org/2000/01/rdf-schema#comment | "The human Y-box protein 1 (YB-1) is a member of the Y-box protein family, a class of proteins involved in transcriptional and translational regulation of a wide range of genes. Here, we report the solution structure of the cold-shock domain (CSD) of YB-1, which is thought to be responsible for nucleic acid binding. It is the first structure solved of a eukaryotic member of the cold-shock protein family and consists of a closed five-stranded anti-parallel beta-barrel capped by a long flexible loop. The structure of CSD is similar to the OB-fold and a comparison with bacterial cold-shock proteins shows that its structural properties are conserved from bacteria to man. Our data suggest the presence of a DNA-binding site consisting of a patch of positively charged and aromatic residues on the surface of the beta-barrel. Further, it is shown that CSD, which has a preference for binding single-stranded pyrimidine-rich sequences, binds weakly and hardly specifically to DNA. Binding affinities reported for intact YB-1 indicate that domains other than the CSD play a role in DNA binding of YB-1."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.2001.5334"xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.2001.5334"xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Hilbers C.W."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Hilbers C.W."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Lasonder E."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Lasonder E."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Grzesiek S."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Grzesiek S."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Hoffmann A."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Hoffmann A."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Vuister G.W."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Vuister G.W."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Kloks C.P.A.M."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Kloks C.P.A.M."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Spronk C.A.E.M."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/author | "Spronk C.A.E.M."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/pages | "317-326"xsd:string |
http://purl.uniprot.org/citations/11851341 | http://purl.uniprot.org/core/pages | "317-326"xsd:string |