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TitleCancer-associated mutations of histones H2B, H3.1 and H2A.Z.1 affect the structure and stability of the nucleosome.
Journal, issue, pagesNucleic Acids Res., Vol. 46, Page 10007-10018, Year 2018
Publish dateJul 16, 2017 (structure data deposition date)
AuthorsArimura, Y. / Ikura, M. / Fujita, R. / Noda, M. / Kobayashi, W. / Horikoshi, N. / Sun, J. / Shi, L. / Kusakabe, M. / Harata, M. ...Arimura, Y. / Ikura, M. / Fujita, R. / Noda, M. / Kobayashi, W. / Horikoshi, N. / Sun, J. / Shi, L. / Kusakabe, M. / Harata, M. / Ohkawa, Y. / Tashiro, S. / Kimura, H. / Ikura, T. / Kurumizaka, H.
External linksNucleic Acids Res. / PubMed:30053102
MethodsX-ray diffraction
Resolution1.99 - 2.45 Å
Structure data

PDB-5y0c:
Crystal Structure of the human nucleosome at 2.09 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.087 Å

PDB-5y0d:
Crystal Structure of the human nucleosome containing the H2B E76K mutant
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-5z30:
The crystal structure of the nucleosome containing a cancer-associated histone H2A.Z R80C mutant
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN/DNA / DNA binding / nucleus / histone fold / chromatin formation / nucleosome / DNA BINDING PROTEIN-DNA complex / histone / chromatin

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