ArticleStructure (London, England : 1993)2024
Structural basis for FN3K-mediated protein deglycation.
Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Protein turnover in plants-cost of synthesis, repair, and crop engineering opportunities.Plant physiology · 2026Review
- Ancestral protein reconstruction reveals the mechanism of substrate specificity in FN3K-mediated deglycation.Communications biology · 2026Article
- Ancestral protein reconstruction reveals the mechanism of substrate specificity in FN3K-mediated deglycation.Research square · 2025Article
- The molecular basis of Human FN3K mediated phosphorylation of glycated substrates.Nature communications · 2025Article
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Authors and funding
6 authors.
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Abstract
Protein glycation is a universal, non-enzymatic modification that occurs when a sugar covalently attaches to a primary amine. These spontaneous modifications may have deleterious or regulatory effects on protein function, and their removal is mediated by the conserved metabolic kinase fructosamine-3-kinase (FN3K). Despite its crucial role in protein repair, we currently have a poor understanding of how FN3K engages or phosphorylates its substrates. By integrating structural biology and biochemistry, we elucidated the catalytic mechanism for FN3K-mediated protein deglycation. Our work identifies key amino acids required for binding and phosphorylating glycated substrates and reveals the molecular basis of an evolutionarily conserved protein repair pathway. Additional structural-functional studies revealed unique structural features of human FN3K as well as differences in the dimerization behavior and regulation of FN3K family members. Our findings improve our understanding of the structure of FN3K and its catalytic mechanism, which opens new avenues for therapeutically targeting FN3K.
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