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. 2023 Mar 30;13:5186. doi: 10.1038/s41598-023-32019-3

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Structural comparison of MMP/N-TIMP2 complexes. Modeled complexes of N-TIMP2 with each MMP are shown, with MMP-2/N-TIMP2 in pink/salmon, MMP-9/N-TIMP2 in pale cyan/pale green, and MMP-14/N-TIMP2 in yellow orange/pale yellow. The MMP catalytic Zn²⁺ is shown as a gray sphere. The H-bond between N-TIMP2-S69 and MMP-14-H249 is shown as a dashed black line, and the relevant residues in both proteins are labeled.