2021
Structural basis for ligand reception by anaplastic lymphoma kinase
Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.Peer-Reviewed Original Research
2006
Structural characterization of autoinhibited c-Met kinase produced by coexpression in bacteria with phosphatase
Wang W, Marimuthu A, Tsai J, Kumar A, Krupka H, Zhang C, Powell B, Suzuki Y, Nguyen H, Tabrizizad M, Luu C, West B. Structural characterization of autoinhibited c-Met kinase produced by coexpression in bacteria with phosphatase. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 3563-3568. PMID: 16537444, PMCID: PMC1450123, DOI: 10.1073/pnas.0600048103.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCrystallography, X-RayCSK Tyrosine-Protein KinaseDNAEscherichia coliGene ExpressionGenetic VectorsModels, MolecularMutationNeoplasmsPhosphotransferasesProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-metRecombinant ProteinsSrc-Family KinasesConceptsC-Met kinaseKinase active siteC-Abl kinaseTyrosine phosphataseUnphosphorylated formSmall molecule compoundsKinase domainProtein kinaseC-SrcActive sitePhosphorylated formC-AblKinaseIntricate networkBicistronic vectorEscherichia coliLarge familyNormal regulationX-ray crystallographyEnzyme activityConformation stateSelective inhibitorDifferent conformation statesPhosphataseInhibitors
2005
Crystal Structures of Proto-oncogene Kinase Pim1: A Target of Aberrant Somatic Hypermutations in Diffuse Large Cell Lymphoma
Kumar A, Mandiyan V, Suzuki Y, Zhang C, Rice J, Tsai J, Artis D, Ibrahim P, Bremer R. Crystal Structures of Proto-oncogene Kinase Pim1: A Target of Aberrant Somatic Hypermutations in Diffuse Large Cell Lymphoma. Journal Of Molecular Biology 2005, 348: 183-193. PMID: 15808862, DOI: 10.1016/j.jmb.2005.02.039.Peer-Reviewed Original ResearchMeSH KeywordsAdenylyl ImidodiphosphateAmino Acid SequenceApoproteinsCrystallography, X-RayHumansLymphoma, Large B-Cell, DiffuseModels, MolecularMolecular Sequence DataMutationProtein BindingProtein ConformationProtein Serine-Threonine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-pim-1Sequence AlignmentConceptsKinase activitySerine/threonine kinaseAberrant somatic hypermutationSomatic hypermutationKinase inhibitor scaffoldN-terminal lobePim1 mutantsTypical kinasesCo-crystal structureThreonine kinaseProtein kinaseBackbone hydrogen bondsKinase PIM1Apo formBiological functionsProline residuesPIM1 inhibitorsNovel chemical classUnique structural featuresLow molecular massInhibitor scaffoldsCell survivalMolecular massPosition 123PIM1
2004
Structural Basis for the Activity of Drugs that Inhibit Phosphodiesterases
Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY. Structural Basis for the Activity of Drugs that Inhibit Phosphodiesterases. Structure 2004, 12: 2233-2247. PMID: 15576036, DOI: 10.1016/j.str.2004.10.004.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCrystallography, X-RayPhosphodiesterase InhibitorsPhosphoric Diester HydrolasesProtein Structure, TertiaryConceptsHigh-resolution crystal structuresInvariant glutamineHydrogen bondingCatalytic domainStructural basisStructural insightsIsoform-selective inhibitorsHydrolysis of cAMPHydrophobic residuesInhibitor bindingActive siteCrystal structureCocrystal structureHydrophobic clampLarge familyDifferent inhibitorsPhosphodiesterasesVariety of diseasesSelective PDE inhibitorsInhibitorsActivity of drugsPDE inhibitorsBondingEnzymeResiduesA Glutamine Switch Mechanism for Nucleotide Selectivity by Phosphodiesterases
Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G. A Glutamine Switch Mechanism for Nucleotide Selectivity by Phosphodiesterases. Molecular Cell 2004, 15: 279-286. PMID: 15260978, DOI: 10.1016/j.molcel.2004.07.005.Peer-Reviewed Original ResearchMeSH Keywords3',5'-Cyclic-AMP Phosphodiesterases3',5'-Cyclic-GMP PhosphodiesterasesCatalytic DomainCrystallography, X-RayCyclic AMPCyclic GMPCyclic Nucleotide Phosphodiesterases, Type 3Cyclic Nucleotide Phosphodiesterases, Type 4Cyclic Nucleotide Phosphodiesterases, Type 5GlutamineHumansModels, MolecularProtein ConformationConceptsNucleotide selectivityKey specificity determinantKey histidine residuesFamily of enzymesHigh-resolution co-crystal structuresCo-crystal structureNew PDE inhibitorsGlutamine switchInvariant glutamineSpecificity determinantsTypes of phosphodiesterasesGlutamine functionsGlutamine residuesHistidine residuesSwitch mechanismStructural understandingPhosphodiesterasesCyclic nucleotidesResiduesCritical rolePurine moietyCGMPCAMPPDE inhibitorsNucleotides