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. Author manuscript; available in PMC: 2021 Feb 28.
Published in final edited form as: Nat Chem Biol. 2020 Aug 31;16(12):1403–1410. doi: 10.1038/s41589-020-0626-6

Figure 2.

Figure 2.

Crystal structure of NSD1 with covalently bound BT3. a) Chemical structure of BT3. b) MS spectrum of 1 μM NSD1 SET domain incubated with 30 μM BT3 for 18 h at 30 °C. Representative spectrum of two independent experiments. c) Crystal structure of NSD1 SET with covalently bound BT3. Electron density omit map for BT3 contoured at 1 σ is shown as black mesh. BT3 and residues in the binding site are shown as sticks; SAM is blue. d) Details of BT3 binding site. BT3 (orange carbons), selected residues in the binding site (white carbons) and SAM (blue carbons) are shown in sticks. Internal water is shown as red sphere. e) Comparison of the autoinhibitory loop regions between NSD1 SET bound to BT3 (left, autoinhibitory loop in magenta) and ligand free NSD1 SET (right, autoinhibitory loop is green). Protein is in surface representation, SAM (green and magenta) and BT3 (blue) are shown in sticks; f) Conformation of the autoinhibitory loop and the C-terminus in NSD1 SET with bound BT3 (magenta carbons) superimposed onto the structure of ligand-free NSD1 SET (green carbons). Selected residues are presented in sticks and labeled.