ArticleArchives of biochemistry and biophysics2012
The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B.
Article in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 78 citations in OpenAlex.
- Article
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- Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.JACS Au · 2026Article
- The Discovery of Abl Kinase ATPase Activity and Its Implications in the Development of Straightforward Assays.ACS omega · 2025Article
- Article
- Mapping allosteric rewiring in related protein structures from collections of crystallographic multiconformer models.bioRxiv : the preprint server for biology · 2025Article
- Native dynamics and allosteric responses in PTP1B probed by high-resolution HDX-MS.Protein science : a publication of the Protein Society · 2024Article
- Allostery in Protein Tyrosine Phosphatases is Enabled by Divergent Dynamics.Journal of chemical information and modeling · 2024Article
- Sequence - dynamics - function relationships in protein tyrosine phosphatases.QRB discovery · 2024Article
- Cancer and Autism: How PTEN Mutations Degrade Function at the Membrane and Isoform Expression in the Human Brain.Journal of molecular biology · 2023Article
- Native dynamics and allosteric responses in PTP1B probed by high-resolution HDX-MS.bioRxiv : the preprint server for biology · 2023Article
- Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases.Chemical science · 2022Article
- Drug Discovery of Plausible Lead Natural Compounds That Target the Insulin Signaling Pathway: Bioinformatics Approaches.Evidence-based complementary and alternative medicine : eCAM · 2022Review
- Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.Biochemistry · 2021Article
- Single Residue on the WPD-Loop Affects the pH Dependency of Catalysis in Protein Tyrosine Phosphatases.JACS Au · 2021Article
- The mechanism of full activation of tumor suppressor PTEN at the phosphoinositide-enriched membrane.iScience · 2021Article
- Are vanadium complexes druggable against the main protease MInorganica chimica acta · 2021Article
- Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases.Journal of the American Chemical Society · 2021Article
- Ligand-Binding-Site Refinement to Generate Reliable Holo Protein Structure Conformations from Apo Structures.Journal of chemical information and modeling · 2021Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The movement of a conserved protein loop (the WPD-loop) is important in catalysis by protein tyrosine phosphatases (PTPs). Using kinetics, isotope effects, and X-ray crystallography, the different effects arising from mutation of the conserved tryptophan in the WPD-loop were compared in two PTPs, the human PTP1B, and the bacterial YopH from Yersinia. Mutation of the conserved tryptophan in the WPD-loop to phenylalanine has a negligible effect on k(cat) in PTP1B and full loop movement is maintained. In contrast, the corresponding mutation in YopH reduces k(cat) by two orders of magnitude and the WPD loop locks in an intermediate position, disabling general acid catalysis. During loop movement the indole moiety of the WPD-loop tryptophan moves in opposite directions in the two enzymes. Comparisons of mammalian and bacterial PTPs reveal differences in the residues forming the hydrophobic pocket surrounding the conserved tryptophan. Thus, although WPD-loop movement is a conserved feature in PTPs, differences exist in the molecular details, and in the tolerance to mutation, in PTP1B compared to YopH. Despite high structural similarity of the active sites in both WPD-loop open and closed conformations, differences are identified in the molecular details associated with loop movement in PTPs from different organisms.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.