Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 71, Issue -, Pages 1423-1432Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1399004715007452
Keywords
high-mobility group protein; X-ray crystallography; DNA binding; HMGB1
Funding
- Structural Biology Shared Resource of the University of Colorado Cancer Center [NIH P30CA046934]
- NIH [R01 GM079154]
- Ministerio de Ciencia e Innovacion [BFU-2009-10380]
- FEDER
- Generalitat de Catalunya [SRG2009-1208]
- CUR del DIUE de la Generalitat de Catalunya i del Fons Social Europeu
- Consejo de Ciencia y Tecnologia (CONACYT) [212993]
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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 of HMGB1 box A bound to an AT-rich DNA fragment is reported at a resolution of 2 angstrom. Two box A domains of HMGB1 collaborate in an unusual configuration in which the Phe37 residues of both domains stack together and intercalate the same CG base pair, generating highly kinked DNA. This represents a novel mode of DNA recognition for HMGB proteins and reveals a mechanism by which structure-specific HMG boxes kink linear DNA.
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