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TitleInvestigation of Trimethyllysine Binding by the HP1 Chromodomain via Unnatural Amino Acid Mutagenesis.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 139, Page 17253-17256, Year 2017
Publish dateAug 27, 2017 (structure data deposition date)
AuthorsBaril, S.A. / Koenig, A.L. / Krone, M.W. / Albanese, K.I. / He, C.Q. / Lee, G.Y. / Houk, K.N. / Waters, M.L. / Brustad, E.M.
External linksJ. Am. Chem. Soc. / PubMed:29111699
MethodsX-ray diffraction
Resolution1.285 - 1.518 Å
Structure data

PDB-6asz:
Chromodomain HP1 with Y24F mutation bound to histone H3 peptide containing trimethyl lysine
Method: X-RAY DIFFRACTION / Resolution: 1.518 Å

PDB-6at0:
Chromodomain HP1 with a p-nitro-L-phenylalanine mutation at position 24 bound to histone H3 peptide containing trimethyl lysine
Method: X-RAY DIFFRACTION / Resolution: 1.285 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • drosophila melanogaster (fruit fly)
KeywordsTRANSCRIPTION / histone reader

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