Publications by authors named "Yeon Seung Park"
Heat shock proteins are induced by activation of heat shock factor 1 (HSF1) in response to heat shock and protect against heat stress. However, the molecular mechanisms underlying the downstream signal of heat shock have not been fully elucidated. We found that similarly to canonical Hsps, Arc/Arg3.
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- CoMsrA is a selenocysteine-containing methionine-S-sulfoxide reductase that typically functions as a monomer but can dimerize during catalysis when interacting with its substrate, methionine sulfoxide.
- The dimerization occurs through an intermolecular disulfide bond between the catalytic Cys16 residues and is dependent on the concentration of the substrate and time.
- Structural analysis shows a unique crystal structure of the dimer with a cone-shaped opening at the interface, highlighting a new mechanism of enzyme catalysis and regeneration involving glutaredoxin.
Protein structures are dynamically changed in response to post-translational modifications, ligand or chemical binding, or protein-protein interactions. Understanding the structural changes that occur in proteins in response to potential candidate drugs is important for predicting the modes of action of drugs and their functions and regulations. Recent advances in hydrogen/deuterium exchange mass spectrometry (HDX-MS) have the potential to offer a tool for obtaining such understanding similarly to other biophysical techniques, such as X-ray crystallography and high resolution NMR.
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