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
1998
Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II
Shao W, Fernandez E, Wilken J, Thompson D, Siani M, West J, Lolis E, Schweitzer B. Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II. FEBS Letters 1998, 441: 77-82. PMID: 9877169, DOI: 10.1016/s0014-5793(98)01520-8.Peer-Reviewed Original ResearchConceptsTotal chemical synthesisNuclear magnetic resonanceChemical synthesisX-ray crystallographyThree-dimensional structureStructural studiesSynthesisSecondary structureGenome programNew proteinsMagnetic resonanceSelenomethionine proteinsRecombinant proteinsProtein IIHeavy-atom derivativesProteinMIP IICrystallographyMonomersStructureDeterminationDerivativesCloningHigh resolutionResonanceSolution 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
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