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. Author manuscript; available in PMC: 2016 Nov 28.
Published in final edited form as: Nature. 2016 Feb 17;530(7591):447–452. doi: 10.1038/nature16952

Figure 3. Interfaces among MLL3SET, RBBP5AS-ABM and ASH2LSPRY.

Figure 3

a, Detailed view of the ASH2LSPRY–RBBP5ABM interface. b, The interface between MLL3SET and RBBP5AS. c, MLL3 Arg4806 forms an extensive salt-bridge and hydrogen-bonding network with ASH2L and RBBP5. d, Mutations of the conserved arginine in MLL proteins disrupt interactions with RBBP5–ASH2L, as shown by the GST pull-down assay in 300 mM NaCl buffer. e, Arginine mutations impair the HKMT activities of MLL family proteins. Activities of all complexes are normalized to the activity of wild-type MLL1–WDR5–RBBP5–ASH2L, and shown as mean ± s.d. (n = 3).