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Structure paper

TitleStructural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders.
Journal, issue, pagesJ. Struct. Biol., Vol. 213, Page 107681-107681, Year 2020
Publish dateAug 24, 2020 (structure data deposition date)
AuthorsOsko, J.D. / Porter, N.J. / Decroos, C. / Lee, M.S. / Watson, P.R. / Raible, S.E. / Krantz, I.D. / Deardorff, M.A. / Christianson, D.W.
External linksJ. Struct. Biol. / PubMed:33316326
MethodsX-ray diffraction
Resolution1.5004765401 - 2.40301779656 Å
Structure data

PDB-7jvu:
Crystal structure of human histone deacetylase 8 (HDAC8) I45T mutation complexed with SAHA
Method: X-RAY DIFFRACTION / Resolution: 1.5004765401 Å

PDB-7jvv:
Crystal structure of human histone deacetylase 8 (HDAC8) E66D/Y306F double mutation complexed with a tetrapeptide substrate
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-7jvw:
Crystal structure of human histone deacetylase 8 (HDAC8) G320R mutation complexed with M344
Method: X-RAY DIFFRACTION / Resolution: 2.40301779656 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-SHH:
OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-B3N:
4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Histone deacetylase / Cornelia de Lange Syndrome (CdLS)

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