title: NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization.
abstract: The human high-affinity copper transporter (hCtr1) is a membrane protein that is predicted to have three transmembrane helices and two methionine-rich metal binding motifs. As an oligomeric polytopic membrane protein, hCtr1 is a challenging system for experimental structure determination. The results of an initial application of solution-state NMR methods to a truncated construct containing residues 45-190 in micelles and site-directed mutagenesis of the two cysteine residues demonstrate that Cys-189 but not Cys-161 is essential for both dimer formation and proper folding of the protein.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
authors.forename: Sangwon
authors.initials: S
authors.lastname: Lee
authors.forename: Stephen B
authors.initials: SB
authors.lastname: Howell
authors.forename: Stanley J
authors.initials: SJ
authors.lastname: Opella
mesh_terms: D027682:Cation Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D000079923:Copper Transporter 1; D003545:Cysteine / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008954:Models, Biological; D008957:Models, Genetic; D017510:Protein Folding
chemical_list: D027682:Cation Transport Proteins; D000079923:Copper Transporter 1; C490079:SLC31A1 protein, human; D003545:Cysteine