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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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Site-directed mutagenesis of N-TIMP2 for incorporation of a NCAA. (A) Chemical structures of 3,4-dihydroxyphenylalanine (L-DOPA) and (8-hydroxyquinolin-3-yl)alanine (HqAla). (B) The available crystal structures of bovine TIMP2 (green) in complex with human MMP-14 (cyan, left) (PDB: 1BUV) and human TIMP2 (green) in complex with human MMP-10 (purple, right) (PDB: 4ILW) are used to illustrate the positions and environment of the mutated residues. The latter complex shows human N-TIMP2 with Ser in position 69. The selected mutated N-TIMP2 positions and their side chains are indicated (oxygen atoms of the side chains are colored in red).