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A comprehensive review of peroxiredoxin 4, a redox protein evolved in oxidative protein folding coupled with hydrogen peroxide detoxification.
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Departments of Pathology and Laboratory Medicine, Kanazawa Medical University, 1-1 Daigaku, Uchinada, Ishikawa, 920-0293, Japan.
Peroxiredoxin (PRDX) primarily employs electrons from thioredoxin in order to reduce peroxides. PRDX4 mainly resides either in the endoplasmic reticulum (ER) lumen or in extracellular spaces. Due to the usage of alternative promoters, a first exon is transcribed from different regions of the Prdx4 gene, which results in two types of mRNAs.
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Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
Cyclopamine, a natural alkaloid, can act as an agonist when it binds to the Cysteine-Rich Domain (CRD) of Smoothened receptor and as an antagonist when it binds to the Transmembrane Domain (TMD). To study the effect of cyclopamine binding to each site experimentally, mutations in the other site are required. Hence, simulations are critical for understanding the WT activity due to binding at different sites.
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View Article and Find Full Text PDFStructure and function of the ROR2 cysteine-rich domain in vertebrate noncanonical WNT5A signaling.
Elife
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The receptor tyrosine kinase ROR2 mediates noncanonical WNT5A signaling to orchestrate tissue morphogenetic processes, and dysfunction of the pathway causes Robinow syndrome, brachydactyly B, and metastatic diseases. The domain(s) and mechanisms required for ROR2 function, however, remain unclear. We solved the crystal structure of the extracellular cysteine-rich (CRD) and Kringle (Kr) domains of ROR2 and found that, unlike other CRDs, the ROR2 CRD lacks the signature hydrophobic pocket that binds lipids/lipid-modified proteins, such as WNTs, suggesting a novel mechanism of ligand reception.
View Article and Find Full Text PDFsubsp. native to the Middle East comprises Pea Albumin1 b-like homologs: A promising natural biopesticide.
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INSA Lyon, INRAE, BF2I, UMR203, 69621 Villeurbanne, France.
The extensive and indiscriminate use of chemical pesticides in agriculture has led to adverse effects on human health, environmental pollution, and the emergence of pesticide-resistant pests. To mitigate these challenges, the development of environmentally friendly alternatives is crucial, with biopesticides emerging as promising solutions such as peptides. Legume seeds naturally contain diverse insecticidal peptides or proteins to combat pest attacks.
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