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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-S69HqAla complexes. (A) Superpositions of the modeled complexes of N-TIMP2-S69HqAla bound to each of the three MMPs are shown, with MMP-2/N-TIMP2-S69HqAla in pink/salmon, MMP-9/N-TIMP2-S69HqAla in pale cyan/pale green, and MMP-14/N-TIMP2-S69HqAla in yellow orange/pale yellow. The MMP catalytic Zn²⁺ is shown as a gray sphere. (B–D) The local environment surrounding HqAla is shown for the complex with MMP-2 (B), MMP-9 (C), or MMP-14 (D). HqAla is represented in magenta, lime, and orange, respectively, with potential H-bonds indicated with black dashed lines. HqAla appears to interact more closely with MMP-2 and MMP-9, whereas a steric clash with Phe204 precludes close interaction with MMP-14.