1H95
Solution structure of the single-stranded DNA-binding Cold Shock Domain (CSD) of human Y-box protein 1 (YB1) determined by NMR (10 lowest energy structures)
Summary for 1H95
Entry DOI | 10.2210/pdb1h95/pdb |
NMR Information | BMRB: 4147 |
Descriptor | Y-BOX BINDING PROTEIN (1 entity in total) |
Functional Keywords | translation factor, transcription factor, ob-fold, 5-stranded anti-parallel beta-barrel, single stranded dna binding, cold shock, y-box |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 1 |
Total formula weight | 8754.90 |
Authors | Kloks, C.P.A.M.,Spronk, C.A.E.M.,Hoffmann, A.,Vuister, G.W.,Grzesiek, S.,Hilbers, C.W. (deposition date: 2001-02-23, release date: 2002-02-21, Last modification date: 2024-05-15) |
Primary citation | Kloks, C.P.A.M.,Spronk, C.A.E.M.,Lasonder, E.,Hoffmann, A.,Vuister, G.W.,Grzesiek, S.,Hilbers, C.W. The Solution Structure and DNA-Binding Properties of the Cold-Shock Domain of the Human Y-Box Protein Yb-1. J.Mol.Biol., 316:317-, 2002 Cited by PubMed Abstract: 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. PubMed: 11851341DOI: 10.1006/JMBI.2001.5334 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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