ArticleComputational and structural biotechnology journal2026
Exploring the Regulatory Function of NGAL in MMP-9 Complexes.
Article in Computational and structural biotechnology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Matrix metalloproteinase 9 (MMP-9) is an enzyme involved in the degradation of the extracellular matrix and in numerous physiological and pathological processes. One of the less understood regulatory mechanisms of MMP-9 is its interaction with neutrophil gelatinase-associated lipocalin (NGAL), leading to the formation of a covalent or noncovalent complex, which may affect the enzyme's activity, its stability, and binding by tissue inhibitors of metalloproteinases (TIMPs), in particular TIMP-1. In this study, molecular modeling was used to investigate the structural basis of NGAL's regulatory effect. Covalent and noncovalent MMP-9/NGAL complexes were constructed and analyzed, as well as the tetrameric inhibitory complex MMP-9/NGAL/TIMP-1/MMP-9. Results indicate that NGAL stabilizes the structure of the hemopexin domain of MMP-9, protecting it from autodegradation. Furthermore, the identified protein interactions may explain the experimentally observed increased affinity of TIMP-1 for the MMP-9/NGAL complex. Comparison with the terminal MMP-9/TIMP-1 complex shows that the presence of NGAL induces slight but reproducible changes in the inhibitory interfaces.
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