2011
Crystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose Octasulfate*
Xue Y, Lee S, Wang Y, Ha Y. Crystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose Octasulfate*. Journal Of Biological Chemistry 2011, 286: 29748-29757. PMID: 21715329, PMCID: PMC3191016, DOI: 10.1074/jbc.m111.219659.Peer-Reviewed Original ResearchConceptsAPP-like proteinsE2 domainHEK-293 cellsSucrose OctasulfateSignal transductionProtein geneBasic residuesSOS moleculesMutational analysisE2 dimerMost residuesProcessing of APPFamilial Alzheimer's diseaseExtracellular matrixAmyloid precursor protein geneProteolysis of APPMissense mutationsProtein 1Key heparinProteinResiduesSymmetry mateAPLP1Precursor protein geneCrystal structure
2007
NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization
Lee S, Howell SB, Opella SJ. NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization. Biochimica Et Biophysica Acta 2007, 1768: 3127-3134. PMID: 17959139, PMCID: PMC2275670, DOI: 10.1016/j.bbamem.2007.08.037.Peer-Reviewed Original ResearchConceptsMembrane proteinsHuman high-affinity copper transporterHigh-affinity copper transporterCys-189Polytopic membrane proteinsSolution-state NMR methodsMetal-binding motifHuman copper transporter 1Site-directed mutagenesisCopper transporter 1Cys-161Transmembrane helicesExperimental structure determinationProper foldingCorrect foldingCopper transporterCysteine residuesBinding motifProteinDimer formationMutagenesisTransporter 1FoldingStructure determinationNMR methods
2003
Structure and dynamics of a membrane protein in micelles from three solution NMR experiments
Lee S, Mesleh MF, Opella SJ. Structure and dynamics of a membrane protein in micelles from three solution NMR experiments. Journal Of Biomolecular NMR 2003, 26: 327-334. PMID: 12815259, DOI: 10.1023/a:1024047805043.Peer-Reviewed Original ResearchConceptsMembrane proteinsSolution NMR experimentsPISA wheelsLoop regionDipolar wavesResidual dipolar couplingsBackbone amide resonancesPf1 coat proteinHigh-throughput structural characterizationHeteronuclear NOE experimentsMembrane-bound formHydrophobic helicesHMQC-NOESY experimentsAmphipathic helixCoat proteinNMR experimentsMobile residuesHelical residuesBackbone dynamicsChemical shift anisotropyProteinAmide resonancesHelixResidual chemical shift anisotropyDipolar couplingsDipolar Waves Map the Structure and Topology of Helices in Membrane Proteins
Mesleh MF, Lee S, Veglia G, Thiriot DS, Marassi FM, Opella SJ. Dipolar Waves Map the Structure and Topology of Helices in Membrane Proteins. Journal Of The American Chemical Society 2003, 125: 8928-8935. PMID: 12862490, PMCID: PMC3272074, DOI: 10.1021/ja034211q.Peer-Reviewed Original ResearchConceptsMembrane proteinsDipolar wavesOrientation of helicesHelical membrane proteinsMolecular frameBilayer samplesMicelle samplesDipolar couplingsAbsolute rotationProteinHelixExperimental measurementsStructured residuesResiduesWavesStructure determinationNMR spectroscopyResidue numberSignificant stepRotationSpectroscopyWave mapsTurn periodCouplingKinks