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. 2018 Jan 5;25(3):600–615. doi: 10.1038/s41418-017-0002-6

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© ADMC Associazione Differenziamento e Morte Cellulare 2018

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License, which permits any non-commercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. If you remix, transform, or build upon this article or a part thereof, you must distribute your contributions under the same license as the original. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/.

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Fig. 4 — Three-dimensional model of sumoylated Notch1 transcription complex. CSL (light green), MAML1 (purple), DNA (orange), ANK repeat domain (cyan), and the N-terminal part (until E1777) of the RAM peptide (cyan) are from the crystal structure of the Notch1 transcription complex (PDB 3V79; 56). The C-terminal part of the RAM peptide (A1778-D1790) containing the sumoylated K1780 (shown as a representative for sumoylation with cyan spheres), K1781 and K1782 was modeled, along with SUMO (green) and the E2-conjugating enzyme Ubc9 (wheat), using the crystal structure of sumoylated Ran GTPase-activating protein 1 (PDB 3UIP; 80) as a template for modeling