2011
Crystal structure of amyloid precursor-like protein 1 and heparin complex suggests a dual role of heparin in E2 dimerization
Xue Y, Lee S, Ha Y. Crystal structure of amyloid precursor-like protein 1 and heparin complex suggests a dual role of heparin in E2 dimerization. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 16229-16234. PMID: 21930949, PMCID: PMC3182750, DOI: 10.1073/pnas.1103407108.Peer-Reviewed Original ResearchThe E2 Domains of APP and APLP1 Share a Conserved Mode of Dimerization
Lee S, Xue Y, Hu J, Wang Y, Liu X, Demeler B, Ha Y. The E2 Domains of APP and APLP1 Share a Conserved Mode of Dimerization. Biochemistry 2011, 50: 5453-5464. PMID: 21574595, PMCID: PMC3120129, DOI: 10.1021/bi101846x.Peer-Reviewed Original ResearchAmino Acid SubstitutionAmyloid beta-Protein PrecursorBinding SitesConserved SequenceCrystallography, X-RayDimerizationHeparinHumansIn Vitro TechniquesModels, MolecularPhosphatesProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant ProteinsStatic Electricity
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