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Title: The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1.
Authors: Kloks, CP
Spronk, CA
Lasonder, E
Hoffmann, A
Vuister, GW
Grzesiek, S
Hilbers, CW
First Published: 15-Feb-2002
Citation: J MOL BIOL, 2002, 316 (2), pp. 317-326
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.
DOI Link: 10.1006/jmbi.2001.5334
ISSN: 0022-2836
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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