Plasticity of Human Protein Disulfide Isomerase
نویسندگان
چکیده
منابع مشابه
Plasticity of Human Protein Disulfide Isomerase
Protein disulfide isomerase (PDI), which consists of multiple domains arranged as abb'xa'c, is a key enzyme responsible for oxidative folding in the endoplasmic reticulum. In this work we focus on the conformational plasticity of this enzyme. Proteolysis of native human PDI (hPDI) by several proteases consistently targets sites in the C-terminal half of the molecule (x-linker and a' domain) lea...
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Protein disulfide isomerase (PDI) composed of four thioredoxin-like domains a, b, b', and a', is a key enzyme catalyzing oxidative protein folding in the endoplasmic reticulum. Large scale molecular dynamics simulations starting from the crystal structures of human PDI (hPDI) in the oxidized and reduced states were performed. The results indicate that hPDI adopts more compact conformations in s...
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Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways in the host-pathogen interaction. These especially affect (i) pathogen entry through protein redox switches and redox modification (i.e., intra-...
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Chao Wang, Sihong Chen, Xi Wang, Lei Wang, A. Katrine Wallis, Robert B. Freedman, and Chih-chen Wang From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, the Graduate University of the Chinese Academy of Sciences, Beijing 100049, China, and the Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, U...
متن کاملOrganocatalysts of oxidative protein folding inspired by protein disulfide isomerase.
Organocatalysts derived from diethylenetriamine effect the rapid isomerization of non-native protein disulfide bonds to native ones. These catalysts contain a pendant hydrophobic moiety to encourage interaction with the non-native state, and two thiol groups with low pKa values that form a disulfide bond with a high E°' value.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.107839