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. 2018 Jun 14;46(14):7138–7152. doi: 10.1093/nar/gky507

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — Structural model of APLF^HBD bound to H2A-H2B using two aromatic anchors. (A) Sequence alignment of APLF^HBD with YL1 used as template for modeling. Cap (c) and anchor (a) residues are indicated, second aromatic residue is indicated with an arrow. (B) Double-anchor model for APLF^HBD bound to H2A-H2B. APLF^HBD in cartoon representation with sidechains shown as sticks. Electrostatic potential is color coded on the Van-der-Waals surface of H2A-H2B. (C) APLF^HBD (surface representation) binds to NMR-derived binding interface and interferes with DNA binding to H2A-H2B. Color coding of CSPs as in Figure 5. (D and E) Close-up views on the two aromatic anchor interactions. Cap-anchor bound to H2B chaperone region in (D), second anchor bound to H2A α1–α2 patch in (E). APLF^HBD in cartoon representation with sidechains shown as sticks. Selected residues and histone SS elements are labeled. Hydrogen bonds indicated with dashes. Green—DNA; cyan—APLF; yellow—H2A; red—H2B.