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. 2021 Apr 25;8(3):1914291. doi: 10.1080/23723556.2021.1914291

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© 2021 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 2. — Structural interface between the acidic domain of Mcl-1 ubiquitin ligase E3 (MULE) and the lysine-rich domain of mouse double minute 2 homolog (MDM2). (a) Surface presentation of the MULE–MDM2 interaction. Models for MULE (residues 2261–2970) and MDM2 (residues 418-491) are generated by high-resolution comparative modeling with the Robetta server,³⁹ and docking analysis performed using the ClusPro server.⁴⁰ (b) Histone deacetylase (HDAC) inhibitor–induced lysine acetylation of MDM2 (at position 466, 467, 469, 470 and 473), leading to MULE dissociation. The acidic domain of MULE (residues 2432-2465) is highlighted in cyan, and the lysine–rich domain of MDM2 (residues 460-476) highlighted in yellow.