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. 2017 Nov 9;7:15121. doi: 10.1038/s41598-017-14754-6

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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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Kinesin α4/α6 inhibitor binding site. (A) Ribbon diagrams. Left, kinesin-5-ADP-BI8 (PDB 3ZCW; α4/α6, dark pink; BI8, dark green). Inset, bound BI8 conformation. Center, KIFC1-ADP (PDB 5WDH; α4/α6, pale blue) superposed with kinesin-5-ADP-BI8. Right, Ncd-ADP H1 (PDB 5W3D; α4/α6, green) superposed with kinesin-5-ADP-BI8. (B) Space-filled α4/α6 cleft. Hydrophobic residues, gray; basic residues, hot pink; acidic residues, green or dark aqua (Ncd). Kinesin-5 G296 and corresponding residues, yellow (KIFC1, G600; Ncd, T607). Center inset, carbon backbone trace of the α4/α6 cleft protein chains.