The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G
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- Schuhmann2022_Article_TheSameButDifferentButStillThe
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Although the general mechanism for serine protease catalysis is well established, some questions still remain. For instance, the two enzymes, neutrophil elastase and cathepsin G, have a lot of structural resemblances. However, elastase degrades virulence factors, while cathepsin G does not. This paper studies both enzymes computationally to probe for their conformational differences. In the process, a methodology is established to not only quantify similarities between the protein trajectories describing proteins' temporal evolution but also account for a varying number of amino acid residues comprising each structure. Our results indicate slight differences in the behavior of the active sites of neutrophil elastase and cathepsin G in the solvent. These subtle changes could indicate differences in the general behavior responsible for the different specificity of the two enzymes.
Originalsprog | Engelsk |
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Artikelnummer | 126 |
Tidsskrift | European Physical Journal D |
Vol/bind | 76 |
Udgave nummer | 7 |
Antal sider | 14 |
ISSN | 1434-6060 |
DOI | |
Status | Udgivet - jul. 2022 |
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