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. 2017 Nov 2;7:14893. doi: 10.1038/s41598-017-14194-2

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits 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. 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/4.0/.

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Importance of the C terminus of the p60-MIT domain for the p60-MIT:p80-CTD complex formation. (A) Superimposition of p60-MIT of the p60-MIT L40P:p80-CTD complex structure (in blue) with the p60-MIT solution NMR structure (PDB ID 2RPA, in grey), and the p60-MIT domain from the katanin:ASPM complex (PDB ID 5LB7, in red). The L40P mutation of p60-MIT that resulted in crystals suitable for structure determination, is highlighted in black. (B) c(S) distribution showing that the minimal version of p60-MIT (aa 1–72 of mouse p60) used to determine its NMR structure does not bind to p80-CTD. For technical reasons, these measurements were carried out with both proteins fused to thioredoxin. All proteins were used at a concentration of 20 µM. (C) Cartoon representation showing the interactions within the C-terminal part of the third helix of p60 that is crucial for p60-MIT:p80-CTD complex formation. Blue, p60-MIT; red, p80-CTD; black, hydrogen bonds. Interacting residues are highlighted as sticks.