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. 2017 Jun 13;7:3385. doi: 10.1038/s41598-017-03457-7

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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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Effect of Nb7 and substrate-like molecules on the conformational flexibility of the 140s loop. (a) Superposition of the structure around the 140s loop with the 2F _o–F _c electron density map at contour level σ = 1 (grey) after soaking crystals containing the muPA:Nb7 complex with EGR-cmk (green) or p-aminobenzamidine (white). (b) An example of a SDS-PAGE analysis of full-length muPA in the absence or presence of Nb7 and the protease Glu-C. The N-terminal sequences of the two pronounced bands at 12 kDa and 15 kDa are indicated to the right. (c) Quantification by densitometry of the band corresponding to the intact catalytic domain of muPA (28 kDa) in the absence or presence of Nb7 and/or EGR-cmk. Error bars, s.d. (n = 3 independent measurements).