The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G
Research output: Contribution to journal › Journal article › Research › peer-review
Documents
- Schuhmann2022_Article_TheSameButDifferentButStillThe
Final published version, 4.5 MB, PDF document
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.
Original language | English |
---|---|
Article number | 126 |
Journal | European Physical Journal D |
Volume | 76 |
Issue number | 7 |
Number of pages | 14 |
ISSN | 1434-6060 |
DOIs | |
Publication status | Published - Jul 2022 |
- OPTIMIZATION, ALIGNMENT, MECHANISM, TARGETS
Research areas
Number of downloads are based on statistics from Google Scholar and www.ku.dk
ID: 315253505