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 ResearchMeSH KeywordsCation Transport ProteinsCloning, MolecularCopper Transporter 1CysteineDimerizationElectrophoresis, Polyacrylamide GelHumansMagnetic Resonance SpectroscopyModels, BiologicalModels, GeneticProtein FoldingConceptsMembrane 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