The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G
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The same, but different, but still the same : structural and dynamical differences of neutrophil elastase and cathepsin G. / Schuhmann, Fabian; Tan, Xiangyin; Gerhards, Luca; Bordallo, Heloisa N.; Solov'yov, Ilia A.
I: European Physical Journal D, Bind 76, Nr. 7, 126, 07.2022.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - The same, but different, but still the same
T2 - structural and dynamical differences of neutrophil elastase and cathepsin G
AU - Schuhmann, Fabian
AU - Tan, Xiangyin
AU - Gerhards, Luca
AU - Bordallo, Heloisa N.
AU - Solov'yov, Ilia A.
PY - 2022/7
Y1 - 2022/7
N2 - 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.
AB - 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.
KW - OPTIMIZATION
KW - ALIGNMENT
KW - MECHANISM
KW - TARGETS
U2 - 10.1140/epjd/s10053-022-00452-0
DO - 10.1140/epjd/s10053-022-00452-0
M3 - Journal article
VL - 76
JO - European Physical Journal D
JF - European Physical Journal D
SN - 1434-6060
IS - 7
M1 - 126
ER -
ID: 315253505