ArticlePloS one2015
Structural Basis for the Specificity of Human NUDT16 and Its Regulation by Inosine Monophosphate.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- NBS1 dePARylation by NUDT16 is critical for DNA double-strand break repair.Molecular and cellular biochemistry · 2025Article
- Roles of nucleotide metabolism in pancreatic cancer.Frontiers in immunology · 2025Review
- NUDT16 regulates CtIP PARylation to dictate homologous recombination repair.Nucleic acids research · 2024Article
- Polyglutamine Expansion in Huntingtin and Mechanism of DNA Damage Repair Defects in Huntington's Disease.Frontiers in cellular neuroscience · 2022Review
- Structural insights into dpCoA-RNA decapping by NudC.RNA biology · 2021Article
- Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates.International journal of molecular sciences · 2021Article
- Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs.Nucleic acids research · 2020Article
- Fluorescent probe displacement assays reveal unique nucleic acid binding properties of human nudix enzymes.Analytical biochemistry · 2020Article
- Article
- Structural analyses of NudT16-ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins.Scientific reports · 2019Article
- Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR.Nature communications · 2018Article
- Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein.Nature structural & molecular biology · 2018Article
- Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides.RNA (New York, N.Y.) · 2018Article
- NUDT expression is predictive of prognosis in patients with clear cell renal cell carcinoma.Oncology letters · 2017Article
- The evolution of function within the Nudix homology clan.Proteins · 2017Article
- Nudix hydrolases degrade protein-conjugated ADP-ribose.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Human NUDT16 is a member of the NUDIX hydrolase superfamily. After having been initially described as an mRNA decapping enzyme, recent studies conferred it a role as an "housecleaning" enzyme specialized in the removal of hazardous (deoxy)inosine diphosphate from the nucleotide pool. Here we present the crystal structure of human NUDT16 both in its apo-form and in complex with its product inosine monophosphate (IMP). NUDT16 appears as a dimer whose formation generates a positively charged trench to accommodate substrate-binding. Complementation of the structural data with detailed enzymatic and biophysical studies revealed the determinants of substrate recognition and particularly the importance of the substituents in position 2 and 6 on the purine ring. The affinity for the IMP product, harboring a carbonyl in position 6 on the base, compared to purine monophosphates lacking a H-bond acceptor in this position, implies a catalytic cycle whose rate is primarily regulated by the product-release step. Finally, we have also characterized a phenomenon of inhibition by the product of the reaction, IMP, which might exclude non-deleterious nucleotides from NUDT16-mediated hydrolysis regardless of their cellular concentration. Taken together, this study details structural and regulatory mechanisms explaining how substrates are selected for hydrolysis by human NUDT16.
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