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- W1980607078 abstract "Proteinase3 (Pr3) is a serine protease of the neutrophils involved in inflammation processes. Its membrane expression is a risk factor for chronic inflammatory diseases such as vasculitis or emphysema. A recent study demonstrated that Pr3 is co-localized with scramblase at the membrane and might thus be related to the externalization of phosphoserine-lipids in apoptotic cells. Biophysical data shows a significant hydrophobic contribution to the binding of Pr3 to lipid bilayers, which is not observed for its close homolog the Human Neutrophil Elastase (HNE). Here, we applied all-atom MD simulations to study the interactions of Pr3 and HNE with equimolar mixtures of DMPC with DMPG, DMPA and DMPS. Pr3 and HNE were introduced into previously calibrated lipid bilayers. These all-atom models enabled us to identify hydrophobic interactions of Pr3 with the lipid tails, which we did not observe for HNE. Further, we identified charge pairing of specific basic residues of Pr3 with DMPS lipids, not found for bilayers containing DMPG or DMPA. Although the substrate specificity of soluble Pr3 has been extensively studied, the influence of the membrane on its enzymatic activity is still a matter of debate. We docked peptides onto our models of membrane-bound Pr3 (mPr3). A thorough comparison of the peptide-protein interactions of mPr3 and soluble Pr3 revealed the changes in Pr3 substrate specificity induced by the membrane. In conclusion, our MD simulations revealed the atomic details of the membrane binding of Pr3, and especially its strong affinity to phosphoserine-lipids. This allows us to propose a hypothesis on the role of Pr3 in apoptosis of neutrophils. In addition, this study contributes to the understanding of the enzymatic activity and substrate specificity of mPr3." @default.
- W1980607078 created "2016-06-24" @default.
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- W1980607078 date "2010-01-01" @default.
- W1980607078 modified "2023-09-29" @default.
- W1980607078 title "The Functional Role of Membrane Bound Proteinase 3" @default.
- W1980607078 doi "https://doi.org/10.1016/j.bpj.2009.12.3086" @default.
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