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. 2018 Mar 1;32(5-6):341–346. doi: 10.1101/gad.311639.118

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© 2018 Zhang et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 1. — The coiled-coil region of DOT1L binds to AF10 and AF17. (A) Schematic diagrams of the domain organization of DOT1L and MLL-AF10. Interactions between DOT1L and AF10 are indicated by a two-way arrow. There are three coiled-coil regions in DOT1L. (B) The coiled-coil region of DOT1L robustly binds to AF10 and AF17 by GST pull-down assay. Triple mutation AF10^{L773D, I777D, L780D} abolishes the DOT1L binding. (C) ITC-based measurements quantifying the binding affinities between the coiled-coil region of DOT1L and AF10^OM-LZ. (NB) No binding. (D) Cartoon representation of the AF10^OM-LZ structure. The two chains are colored cyan and green, respectively. The residues involved in the dimer interface are shown in stick representations. (E) Size exclusion chromatography coupled with multiangle light-scattering analysis of AF10^OM-LZ.