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Structure paper

TitleUnexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach.
Journal, issue, pagesChem. Commun. (Camb. ), Vol. 59, Page 8696-8699, Year 2023
Publish dateDec 1, 2022 (structure data deposition date)
AuthorsPerrin, M.E. / Li, B. / Mbianda, J. / Bakail, M. / Andre, C. / Moal, G. / Legrand, P. / Ropars, V. / Douat, C. / Ochsenbein, F. / Guichard, G.
External linksChem. Commun. (Camb. ) / PubMed:37347155
MethodsX-ray diffraction
Resolution2.127 - 3 Å
Structure data

PDB-8bv1:
Peptide inhibitor P4 in complex with ASF1 histone chaperone
Method: X-RAY DIFFRACTION / Resolution: 2.834 Å

PDB-8cj1:
Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone
Method: X-RAY DIFFRACTION / Resolution: 2.564 Å

PDB-8cj2:
Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
Method: X-RAY DIFFRACTION / Resolution: 2.127 Å

PDB-8cj3:
Urea-based foldamer inhibitor c3u_7 chimera in complex with ASF1 histone chaperone
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsCHAPERONE / Inhibitor / ASF1 / Histone / protein-protein interaction

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