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. Author manuscript; available in PMC: 2022 Jun 24.
Published in final edited form as: J Med Chem. 2021 May 17;64(12):8510–8522. doi: 10.1021/acs.jmedchem.1c00430

Table 1.

Binding of H3K36me3 Variants to PHF1 Tudora

Histone Residues Peptide Sequence ITC Kd (μM)a
H3(33-40) GGVKme3KPHR 22.3 ± 1.9
H3(33-39) GGVKme3KPH 52.0 ± 6.1
H3(33-39)b VGVKme3KPH 48.0 ± 0.2
H3(33-39)b VGVKme3KPL 16.3 ± 3.0
H3(33-40)b GGVKme3KPLR 18.7 ± 4.1
a

Kd values were determined by two independent ITC experiments (mean ± SD).

b

Peptide sequence differs from natural histone H3 sequence at residues denoted in blue.