ArticleScientific reports2017
Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 61 citations in OpenAlex.
- From activation to desensitization: How ABA balances plant growth and abiotic stress response?Plant communications · 2026Review
- Discovery of a sulfotyrosine-motif in the human TrkB extracellular domain required for agonist activation.bioRxiv : the preprint server for biology · 2026Article
- Enhancing Enzymatic Bioconjugation Efficiency via Computer-Based Installation of a Substrate Recruitment Domain.Bioconjugate chemistry · 2026Article
- Structural characterization of metal binding in human tyrosylprotein sulfotransferase 2, TPST2.Scientific reports · 2026Article
- Understanding peptide hormones: from precursor proteins to bioactive molecules.Trends in biochemical sciences · 2025Review
- In silico ligand self-assembly drives binding recognition of natural products intoIn silico pharmacology · 2025Article
- Genome-wide CRISPR screening identifies tyrosylprotein sulfotransferase-2 as a target for augmenting anti-PD1 efficacy.Molecular cancer · 2024Article
- Genome mining of sulfonated lanthipeptides reveals unique cyclic peptide sulfotransferases.Acta pharmaceutica Sinica. B · 2024Article
- Enhanced tyrosine sulfation is associated with chronic kidney disease-related atherosclerosis.BMC biology · 2023Article
- Engineering of SH2 Domains for the Recognition of Protein Tyrosine O-Sulfation Sites.Methods in molecular biology (Clifton, N.J.) · 2023Article
- From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function.Drug metabolism and disposition: the biological fate of chemicals · 2022Review
- Posttranslational modifications of α-conotoxins: sulfotyrosine and C-terminal amidation stabilise structures and increase acetylcholine receptor binding.RSC medicinal chemistry · 2021Article
- Engineering of a Small Protein Scaffold To Recognize Sulfotyrosine with High Specificity.ACS chemical biology · 2021Article
- Structure-based design of nucleoside-derived analogues as sulfotransferase inhibitors.RSC advances · 2019Article
- Sulfation pathways from red to green.The Journal of biological chemistry · 2019Review
- New tools for evaluating protein tyrosine sulfation and carbohydrate sulfation.The Biochemical journal · 2018Review
- New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors.The Biochemical journal · 2018Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechanism of the tyrosine sulfation reaction. However, detailed molecular mechanisms underlying how TPSTs catalyse a variety of substrate proteins with different efficiencies and how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolved. Here, we report two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TPST1 with significantly different efficiencies. The distinct binding modes found in the two complexes provide insight into the sulfation mechanism for these substrates. The present study provides valuable information describing the molecular mechanism of post-translational protein modifications catalysed by TPSTs.
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