2001
CCR2 and CCR5 receptor‐binding properties of herpesvirus‐8 vMIP‐II based on sequence analysis and its solution structure
Shao W, Fernandez E, Sachpatzidis A, Wilken J, Thompson D, Schweitzer B, Lolis E. CCR2 and CCR5 receptor‐binding properties of herpesvirus‐8 vMIP‐II based on sequence analysis and its solution structure. The FEBS Journal 2001, 268: 2948-2959. PMID: 11358512, DOI: 10.1046/j.1432-1327.2001.02184.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesChemokinesChemokines, CCDimerizationEpitopesMagnetic Resonance SpectroscopyModels, ChemicalModels, MolecularMolecular Sequence DataPeptide BiosynthesisProtein BindingProtein ConformationProtein FoldingProtein Structure, SecondaryReceptors, CCR2Receptors, CCR5Receptors, ChemokineSequence Analysis, ProteinSequence Homology, Amino AcidConceptsHuman herpesvirus 8VMIP-IIChemokine receptorsCC chemokinesReceptor-binding propertiesNumerous chemokine receptorsPresence of epitopesHIV-1 viral entryHuman CC chemokineReceptor CCR2Kaposi's sarcomaHerpesvirus 8Infectious agentsCCR2Viral entryReceptor bindingReceptor specificityCCR5ChemokinesSarcomaReceptorsReceptor subfamiliesMagnetic resonanceBroad receptor specificityProtein II
2000
Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation † , ‡
Fernandez E, Wilken J, Thompson D, Peiper S, Lolis E. Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation † , ‡. Biochemistry 2000, 39: 12837-12844. PMID: 11041848, DOI: 10.1021/bi001166f.Peer-Reviewed Original ResearchAmino Acid SequenceAnti-HIV AgentsChemokine CCL11Chemokine CCL5Chemokine CCL7ChemokinesChemokines, CCChemotactic Factors, EosinophilCrystallography, X-RayCytokinesHerpesvirus 8, HumanHumansModels, MolecularMolecular Sequence DataMonocyte Chemoattractant ProteinsReceptors, CCR3Receptors, ChemokineReceptors, VirusSequence AlignmentSequence Homology, Amino Acid
1999
Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡
Sachpatzidis A, Dealwis C, Lubetsky J, Liang P, Anderson K, Lolis E. Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡. Biochemistry 1999, 38: 12665-12674. PMID: 10504236, DOI: 10.1021/bi9907734.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayEnzyme InhibitorsHydrogen BondingModels, MolecularOrganophosphonatesTryptophan SynthaseConceptsTransition stateShort hydrogen bondsTryptophan synthaseHigh conformational flexibilityTetrahedral transition stateTransition state analogueMechanism of catalysisEnzyme-inhibitor complexStructure-based approachPhosphonate oxygenIndole-3-glycerol phosphateHydroxyl oxygenHydrogen bondsSulfur atomsActive siteC3 atomC2 atomCrystal structureConformational flexibilityCrystallographic studiesInhibitor bindingConformation changeAtomsNew herbicidesGlu-49
1998
Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
Swope M, Sun H, Blake P, Lolis E. Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. The EMBO Journal 1998, 17: 3534-3541. PMID: 9649424, PMCID: PMC1170690, DOI: 10.1093/emboj/17.13.3534.Peer-Reviewed Original ResearchConceptsN-terminal prolineN-terminal regionStructure-based inhibitorsMultiple sequence alignmentThree-dimensional structureInvariant residuesEntire polypeptideMicrobial enzymesCatalytic basePro-1Sequence alignmentMIF homologuesCytokine activityHuman macrophage migration inhibitory factorCatalytic siteProlineInhibitory factorHomologuesUnderlying biological activityP-hydroxyphenylpyruvateProteinMacrophage migration inhibitory factorActive siteBiological activityMacrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*
Swope M, Sun H, Klockow B, Blake P, Lolis E. Macrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*. Journal Of Biological Chemistry 1998, 273: 14877-14884. PMID: 9614090, DOI: 10.1074/jbc.273.24.14877.Peer-Reviewed Original ResearchBinding SitesCircular DichroismEnzyme InhibitorsFluorescenceGlutathioneHumansHydrogen-Ion ConcentrationIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein ConformationProtein FoldingRecombinant ProteinsSulfhydryl CompoundsSolution Structure of Murine Macrophage Inflammatory Protein-2 † , ‡
Shao W, Jerva L, West J, Lolis E, Schweitzer B. Solution Structure of Murine Macrophage Inflammatory Protein-2 † , ‡. Biochemistry 1998, 37: 8303-8313. PMID: 9622482, DOI: 10.1021/bi980112r.Peer-Reviewed Original Research
1994
Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
Joseph-McCarthy D, Lolis E, Komives E, Petsko G. Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site. Biochemistry 1994, 33: 2815-23. PMID: 8130194, DOI: 10.1021/bi00176a010.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesCrystallizationCrystallography, X-RayDNA PrimersLigandsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPoint MutationProtein FoldingProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiaeTriose-Phosphate IsomeraseX-Ray DiffractionConceptsMutant enzymesSubstrate-binding loopActive-site LysLys-12Wild-type enzymeMet side chainsActive siteEnzyme-inhibitor complexThree-dimensional structureMutant structuresWild typeTriosephosphate isomeraseDianionic substrateEnzymeSame crystal formCrystal structureMET mutationsSide chainsIsomeraseSitesCrystal formsMutationsPhosphoglycolohydroxamateMethionine
1991
Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
Komives E, Chang L, Lolis E, Tilton R, Petsko G, Knowles J. Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Biochemistry 1991, 30: 3011-9. PMID: 2007138, DOI: 10.1021/bi00226a005.Peer-Reviewed Original Research
1990
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Lolis E, Alber T, Davenport R, Rose D, Hartman F, Petsko G. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 1990, 29: 6609-18. PMID: 2204417, DOI: 10.1021/bi00480a009.Peer-Reviewed Original ResearchConceptsHydrogen bonding interactionsYeast triosephosphate isomeraseActive site structureNon-hydrogen atomsWater moleculesActive siteActive site residuesDrug designGlu-165Triosephosphate isomeraseSite structureCatalytic baseCrystal contactsSite residuesR factorTIM structuresFlexible loopLys-12Polypeptide chainStructureSubunit interfaceCarboxylateMonomersHydroxylFirst timeCrystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Lolis E, Petsko G. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. Biochemistry 1990, 29: 6619-25. PMID: 2204418, DOI: 10.1021/bi00480a010.Peer-Reviewed Original ResearchConceptsHydrogen bondsSide chainsGlu-165Triosephosphate isomeraseLatter hydrogen bondTransition state analogueFinal R factorEnzyme-inhibitor complexSpectroscopic resultsActive siteConformational changesCrystallographic analysisLoop movesPhosphoglycolic acidIsomeraseUnbound formCatalysisR factorBondsEnzymeComplexesStructural termsAtomic modelBindingChain
1987
Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
Alber T, Davenport R, Giammona D, Lolis E, Petsko G, Ringe D. Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme? Cold Spring Harbor Symposia On Quantitative Biology 1987, 52: 603-13. PMID: 3331346, DOI: 10.1101/sqb.1987.052.01.069.Peer-Reviewed Original Research