1997
Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding
Huang H, Horiuchi A, Goldberg J, Greengard P, Nairn A. Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3530-3535. PMID: 9108010, PMCID: PMC20473, DOI: 10.1073/pnas.94.8.3530.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Site-directed mutagenesisActive site residuesOkadaic acidPhosphatase 1Calyculin AMammalian protein phosphatase 1PP-1Site residuesEnzyme activityMutation of residuesAmino acid residuesMechanism of catalysisActive siteInhibitor bindingAcid residuesInhibitory proteinMutationsResiduesMutagenesisDivalent cationsToxinY272Large lossesR221Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
Kwon Y, Huang H, Desdouits F, Girault J, Greengard P, Nairn A. Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3536-3541. PMID: 9108011, PMCID: PMC20474, DOI: 10.1073/pnas.94.8.3536.Peer-Reviewed Original ResearchConceptsPP-1cPP-1C.PP-1DARPP-32Inhibitor 2Protein phosphatase 1Amino acid sequence analysisAmino acid residuesNH2-terminal regionAcid sequence analysisPhosphoinhibitor-1Threonine residuesPhosphatase 1Inhibitor-1Catalytic subunitCalyculin AOkadaic acidInhibitor proteinActive siteAcid residuesSequence analysisProteinEnzyme activityMotifResidues
1995
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
Goldberg J, Huang H, Kwon Y, Greengard P, Nairn A, Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 1995, 376: 745-753. PMID: 7651533, DOI: 10.1038/376745a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCatalysisCrystallography, X-RayDopamine and cAMP-Regulated Phosphoprotein 32Escherichia coliHumansIntracellular Signaling Peptides and ProteinsMetalsMicrocystinsModels, MolecularMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsPeptides, CyclicPhosphoprotein PhosphatasesPhosphoproteinsProtein ConformationProtein Phosphatase 1ProteinsRabbitsRecombinant ProteinsRNA-Binding ProteinsSequence Homology, Amino AcidConceptsPhosphatase 1Protein serine/threonine phosphatase-1Serine/threonine phosphatase 1Mammalian protein phosphatase 1Protein phosphatase 1Potential binding sitesThree-dimensional structureCatalytic subunitRegulatory sequencesCatalytic domainCarboxy terminusΒ scaffoldBinding sitesActive siteSurface groovesTerminusSubunitsDomainProteinCrystal structureSitesTyrosineMetalloenzymesSequenceToxin