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Structure paper

TitleHPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.
Journal, issue, pagesNat Commun, Vol. 12, Page 1028-1028, Year 2021
Publish dateMar 3, 2020 (structure data deposition date)
AuthorsSun, F.H. / Zhao, P. / Zhang, N. / Kong, L.L. / Wong, C.C.L. / Yun, C.H.
External linksNat Commun / PubMed:33589610
MethodsX-ray diffraction
Resolution1.57 - 1.98 Å
Structure data

PDB-6m3g:
Crystal structure of human HPF1
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-6m3h:
Crystal structure of mouse HPF1
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-6m3i:
Crystal structure of HPF1/PARP1 complex
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-UNU:
BENZAMIDE

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsNUCLEAR PROTEIN / cofactor / ADP-ribosylation / DNA damage response / complex

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