FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2016987675> ?p ?o ?g. }

• W2016987675 endingPage "1690" @default.
• W2016987675 startingPage "1681" @default.
• W2016987675 abstract "The suppressors of T cell receptor (TCR) signaling 1 and 2 (Sts-1 and -2, respectively) are multidomain proteins that negatively regulate the signaling of membrane-bound receptors, including TCR and the epidermal growth factor receptor (EGFR). Sts-1 was recently shown to be a new type of protein tyrosine phosphatase (PTP), with the phosphatase activity located within its C-terminal phosphoglycerate mutase (PGM) homology domain and key for the regulation of TCR signaling in T cells. The activity of the related Sts-2 enzyme is significantly less than that of Sts-1. Here we investigate the phosphatase activity of the PGM domain of Sts-2, Sts-2(PGM). The crystal structure of Sts-2(PGM) is remarkably similar to Sts-1(PGM), including conservation of all catalytic residues. Insight into mechanistic details is provided by the structures of the apo, tungstate-bound, and phosphate-bound enzyme. The active site shows stringent specificity, with the k(cat) optimum at pH 5.0 suggesting that Sts-2 might function as an acid-dependent phosphatase. Mutation of active site residues Gln372, Ala446, Glu481, Ser552, and Ser582 to their equivalents in Sts-1 increases the phosphatase activity of Sts-2(PGM) toward model substrates. Overall, our data demonstrate that Sts-2(PGM) adopts the conformation of an active phosphatase whose activity is fundamentally different from that of Sts-1 despite the strong structural homology. They also demonstrate that nonconserved active site residues are responsible for the difference in activity between the two isoforms. These differences reflect possible distinct physiological substrates." @default.
• W2016987675 created "2016-06-24" @default.
• W2016987675 creator A5006483742 @default.
• W2016987675 creator A5019385496 @default.
• W2016987675 creator A5060958735 @default.
• W2016987675 creator A5067052365 @default.
• W2016987675 date "2009-02-05" @default.
• W2016987675 modified "2023-09-25" @default.
• W2016987675 title "Structural and Functional Characterization of the 2H-Phosphatase Domain of Sts-2 Reveals an Acid-Dependent Phosphatase Activity" @default.
• W2016987675 cites W1639582946 @default.
• W2016987675 cites W1783326107 @default.
• W2016987675 cites W1965975711 @default.
• W2016987675 cites W1967194316 @default.
• W2016987675 cites W1967368177 @default.
• W2016987675 cites W1969918683 @default.
• W2016987675 cites W1982762561 @default.
• W2016987675 cites W1989899886 @default.
• W2016987675 cites W1996607909 @default.
• W2016987675 cites W2013083986 @default.
• W2016987675 cites W2014694459 @default.
• W2016987675 cites W2023627293 @default.
• W2016987675 cites W2027319387 @default.
• W2016987675 cites W2032878806 @default.
• W2016987675 cites W2043617798 @default.
• W2016987675 cites W2071908913 @default.
• W2016987675 cites W2085090715 @default.
• W2016987675 cites W2090236692 @default.
• W2016987675 cites W2094416835 @default.
• W2016987675 cites W2095296343 @default.
• W2016987675 cites W2098854471 @default.
• W2016987675 cites W2099365295 @default.
• W2016987675 cites W2104418929 @default.
• W2016987675 cites W2117962961 @default.
• W2016987675 cites W2126924068 @default.
• W2016987675 cites W2127517334 @default.
• W2016987675 cites W2131350133 @default.
• W2016987675 cites W2133308354 @default.
• W2016987675 cites W2134018306 @default.
• W2016987675 cites W2148414191 @default.
• W2016987675 cites W2161528588 @default.
• W2016987675 cites W4246916591 @default.
• W2016987675 doi "https://doi.org/10.1021/bi802219n" @default.
• W2016987675 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2880635" @default.
• W2016987675 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19196006" @default.
• W2016987675 hasPublicationYear "2009" @default.
• W2016987675 type Work @default.
• W2016987675 sameAs 2016987675 @default.
• W2016987675 citedByCount "25" @default.
• W2016987675 countsByYear W20169876752012 @default.
• W2016987675 countsByYear W20169876752013 @default.
• W2016987675 countsByYear W20169876752015 @default.
• W2016987675 countsByYear W20169876752016 @default.
• W2016987675 countsByYear W20169876752017 @default.
• W2016987675 countsByYear W20169876752018 @default.
• W2016987675 countsByYear W20169876752019 @default.
• W2016987675 countsByYear W20169876752020 @default.
• W2016987675 countsByYear W20169876752022 @default.
• W2016987675 countsByYear W20169876752023 @default.
• W2016987675 crossrefType "journal-article" @default.
• W2016987675 hasAuthorship W2016987675A5006483742 @default.
• W2016987675 hasAuthorship W2016987675A5019385496 @default.
• W2016987675 hasAuthorship W2016987675A5060958735 @default.
• W2016987675 hasAuthorship W2016987675A5067052365 @default.
• W2016987675 hasBestOaLocation W20169876752 @default.
• W2016987675 hasConcept C119795356 @default.
• W2016987675 hasConcept C170493617 @default.
• W2016987675 hasConcept C178666793 @default.
• W2016987675 hasConcept C181199279 @default.
• W2016987675 hasConcept C185592680 @default.
• W2016987675 hasConcept C19317047 @default.
• W2016987675 hasConcept C20251656 @default.
• W2016987675 hasConcept C21547065 @default.
• W2016987675 hasConcept C2776090121 @default.
• W2016987675 hasConcept C41183919 @default.
• W2016987675 hasConcept C54355233 @default.
• W2016987675 hasConcept C55493867 @default.
• W2016987675 hasConcept C85528070 @default.
• W2016987675 hasConcept C86803240 @default.
• W2016987675 hasConcept C8891405 @default.
• W2016987675 hasConcept C91754966 @default.
• W2016987675 hasConceptScore W2016987675C119795356 @default.
• W2016987675 hasConceptScore W2016987675C170493617 @default.
• W2016987675 hasConceptScore W2016987675C178666793 @default.
• W2016987675 hasConceptScore W2016987675C181199279 @default.
• W2016987675 hasConceptScore W2016987675C185592680 @default.
• W2016987675 hasConceptScore W2016987675C19317047 @default.
• W2016987675 hasConceptScore W2016987675C20251656 @default.
• W2016987675 hasConceptScore W2016987675C21547065 @default.
• W2016987675 hasConceptScore W2016987675C2776090121 @default.
• W2016987675 hasConceptScore W2016987675C41183919 @default.
• W2016987675 hasConceptScore W2016987675C54355233 @default.
• W2016987675 hasConceptScore W2016987675C55493867 @default.
• W2016987675 hasConceptScore W2016987675C85528070 @default.
• W2016987675 hasConceptScore W2016987675C86803240 @default.
• W2016987675 hasConceptScore W2016987675C8891405 @default.
• W2016987675 hasConceptScore W2016987675C91754966 @default.
• W2016987675 hasIssue "8" @default.
• W2016987675 hasLocation W20169876751 @default.

• next