Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
- 18 March 1993
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 362 (6417) , 219-223
- https://doi.org/10.1038/362219a0
Abstract
The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 Å resolution by multiwavelength anomalous diffraction on crystals of the selenomethionyl protein. The structure shows a striking similarity to the DNA-binding domain of the catabolite gene activator protein CAP, thereby providing a possible model for the binding of GH5 to DNA.Keywords
This publication has 45 references indexed in Scilit:
- Co-operative binding of the globular domain of histone H5 to DNAJournal of Molecular Biology, 1992
- Site-directed mutagenesis studies on the binding of the globular domain of linker histone H5 to the nucleosomeJournal of Molecular Biology, 1992
- Crystallization of the globular domain of histone H5Journal of Molecular Biology, 1990
- Chromatin superstructure-dependent crosslinking with DNA of the histone H5 residues Thr1, His25 and His62Journal of Molecular Biology, 1990
- Histone H5 in the Control of DNA Synthesis and Cell ProliferationScience, 1989
- Surface, subunit interfaces and interior of oligomeric proteinsJournal of Molecular Biology, 1988
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- A decapeptide motif for binding to the minor groove of DNA A proposalFEBS Letters, 1988
- Complete amino acid sequence of goose erythrocyte H5 histone and the homology between H1 and H5 histonesBiochemical and Biophysical Research Communications, 1979
- Synthesis and turnover of DNA-bound histone during maturation of avian red blood cellsJournal of Molecular Biology, 1972