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Two high-mobility group box domains act together to underwind and kink DNA.

Author
Sanchez, R.; Acosta, F.J.; Malarkey, C.S.; Saperas, N.; Churchill, M.E.A.; Campos, J.Lourdes
Type of activity
Journal article
Journal
Acta crystallographica. Section D, biological crystallography
Date of publication
2015-07-02
Volume
D71
Number
part 7
First page
1423
Last page
1432
DOI
https://doi.org/10.1107/S1399004715007452 Open in new window
Repository
http://hdl.handle.net/2117/78117 Open in new window
URL
http://journals.iucr.org/d/issues/2015/07/00/mh5175/mh5175.pdf Open in new window
Abstract
High-mobility group protein 1 (HMGB1) is an essential and ubiquitous DNA architectural factor that influences a myriad of cellular processes. HMGB1 contains two DNA-binding domains, box A and box B, which have little sequence specificity but have remarkable abilities to underwind and bend DNA. Although HMGB1 box A is thought to be responsible for the majority of HMGB1-DNA interactions with pre-bent or kinked DNA, little is known about how it recognizes unmodified DNA. Here, the crystal structure...
Citation
Sanchez, R., Acosta, F.J., Malarkey, C.S., Saperas, N., Churchill, M.E.A., Campos, J.Lourdes. Two high-mobility group box domains act together to underwind and kink DNA.. "Acta crystallographica. Section D, biological crystallography", 02 Juliol 2015, vol. D71, núm. part 7, p. 1423-1432.
Keywords
4-way junction dna, DNA binding, High-mobility group protein, X-ray crystallography, a-domain, binding proteins, chromatin, cisplatin-modified dna, duplex dna, histone h1, hmgb1, intercalating residues, mitochondrial transcription factor, tandem hmg boxes
Group of research
CEBIM - Molecular Biotechnology Centre
MACROM - Crystallography, Structure and Function of Biological Macromolecules

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