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. 2016 Aug 22;14(1):17. doi: 10.1186/s12964-016-0140-3

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — Detailed view of the complementary surfaces of the CASKIN2 SAM tandem, following the same color scheme as Fig. 3. a Cartoon representation of the five helices comprising each SAM domain, and the location of the complementary head (H) to tail (T) surfaces. The head surface is formed by contributions from helices 2, 3, and 4. The tail surface is formed by contributions mainly from helix 5. b Intermolecular contacts between at the intra- and intermolecular head and tail surfaces are labeled. Boxes indicated amino acids selected for mutagenesis