Protein Disulfide Isomerase and Host-Pathogen Interaction
نویسندگان
چکیده
منابع مشابه
Protein Disulfide Isomerase and Host-Pathogen Interaction
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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ABDUL HANNAN BASIT, WAJID ARSHAD ABBASI, AMINA ASIF, AND FAYYAZ UL AMIR AFSAR MINHAS † Biomedical Informatics Research Laboratory, Department of Computer and Information Sciences, Pakistan Institute of Engineering and Applied Sciences (PIEAS), Nilore, Islamabad, Pakistan Department of Electrical Engineering, Pakistan Institute of Engineer-ing and Applied Sciences (PIEAS), Nilore, Islamabad, 440...
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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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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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During oxidative protein folding, efficient catalysis of disulfide rearrangements by protein-disulfide isomerase is found to involve an escape mechanism that prevents the enzyme from becoming trapped in covalent complexes with substrates that fail to rearrange in a timely fashion. Protein-disulfide isomerase mutants with only a single active-site cysteine catalyze slow disulfide rearrangements ...
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ژورنال
عنوان ژورنال: The Scientific World JOURNAL
سال: 2011
ISSN: 1537-744X
DOI: 10.1100/2011/289182