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. 2015 Nov 15;29(22):2337–2342. doi: 10.1101/gad.270926.115

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© 2015 Wu 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. — Overall structure of the NRMT1–SAH–CENP-A ternary complex. (A) Topology of NRMT1. (Slate blue) Helices; (pink) β strands. CENP-A- and SAH-binding motifs are shaded yellow and green, respectively. CENP-A-interacting loops (L_C, L₄, L_AB, and L₆₇) are highlighted in cyan. (B) NRMT1 in complex with SAH and dimethylated CENP-A peptide. The CENP-A peptide and SAH are depicted as sticks. Color coding is the same as in A. (C) Composition of the CENP-A platform. Several segments of NRMT1 constitute the CENP-A peptide-binding pocket, including N-terminal helices (slate blue), loop L₄ (green), β_AB hairpin (wheat), and loop L₆₇ (cyan). (D) Interaction details that enable an intimate integration of the CENP-A platform. Key residues are shown as sticks and are color-coded in the background of cartoon.