ArticleThe Journal of biological chemistry2010
Insights into the reaction of protein-tyrosine phosphatase 1B: crystal structures for transition state analogs of both catalytic steps.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed.
- NMR relaxation dispersion reveals an order of magnitude range of acid loop motions in protein tyrosine phosphatase 1B.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Lysosome-related organelles employ divergent mechanisms to modulate cytosolic zinc homeostasis.PLoS genetics · 2026Article
- Machine learning-based QSAR and molecular modeling identify promising PTP1B modulators from Ocimum gratissimum for type 2 diabetes therapy.Molecular diversity · 2026Article
- Cancer-Causing Mutations Alter the Interplay Between Loop Dynamics and Catalysis in the Protein Tyrosine Phosphatases SHP-1 and SHP-2.bioRxiv : the preprint server for biology · 2026Article
- Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.JACS Au · 2026Article
- Phosphorylation of a conserved aspartate in the catalytic site of eukaryotic elongation factor 2 kinase.Protein science : a publication of the Protein Society · 2026Article
- WatCon: A Python Tool for Analysis of Conserved Water Networks Across Protein Families.JACS Au · 2025Article
- Distal Mutations Rewire Allosteric Networks to Control Substrate Specificity in PTP1B.Biochemistry · 2025Article
- The Discovery of Abl Kinase ATPase Activity and Its Implications in the Development of Straightforward Assays.ACS omega · 2025Article
- Binding Zinc and Oxo-Vanadium Insulin-Mimetic Complexes to Phosphatase Enzymes: Structure, Electronics and Implications.Molecules (Basel, Switzerland) · 2025Article
- SHP-1 Variants Broaden the Understanding of pH-Dependent Activities in Protein Tyrosine Phosphatases.JACS Au · 2024Article
- Review
- Structural analysis of PTPN21 reveals a dominant-negative effect of the FERM domain on its phosphatase activity.Science advances · 2024Article
- Allostery in Protein Tyrosine Phosphatases is Enabled by Divergent Dynamics.Journal of chemical information and modeling · 2024Article
- MultiscaleJournal of chemical information and modeling · 2024Article
- High-resolution double vision of the allosteric phosphatase PTP1B.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structural and kinetic characterization of DUSP5 with a Di-phosphorylated tripeptide substrate from the ERK activation loop.Frontiers in chemical biology · 2024Article
- Loop dynamics and the evolution of enzyme activity.Nature reviews. Chemistry · 2023Review
- A small molecule inhibitor of PTP1B and PTPN2 enhances T cell anti-tumor immunity.Nature communications · 2023Article
- Deconstructing allostery by computational assessment of the binding determinants of allosteric PTP1B modulators.Communications chemistry · 2023Article
12 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
Catalysis by protein-tyrosine phosphatase 1B (PTP1B) occurs through a two-step mechanism involving a phosphocysteine intermediate. We have solved crystal structures for the transition state analogs for both steps. Together with previously reported crystal structures of apo-PTP1B, the Michaelis complex of an inactive mutant, the phosphoenzyme intermediate, and the product complex, a full picture of all catalytic steps can now be depicted. The transition state analog for the first catalytic step comprises a ternary complex between the catalytic cysteine of PTP1B, vanadate, and the peptide DADEYL, a fragment of a physiological substrate. The equatorial vanadate oxygen atoms bind to the P-loop, and the apical positions are occupied by the peptide tyrosine oxygen and by the PTP1B cysteine sulfur atom. The vanadate assumes a trigonal bipyramidal geometry in both transition state analog structures, with very similar apical O-O distances, denoting similar transition states for both phosphoryl transfer steps. Detailed interactions between the flanking peptide and the enzyme are discussed.
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