NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization.

Stephen B Howell, Stanley J Opella, Sangwon Lee

Journal: Biochimica et biophysica acta 2008;1768(12):3127-34

PMID: 17959139

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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.

Address: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

DOI: 10.1016/j.bbamem.2007.08.037

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https://antibodies.cancer.gov/detail/CPTC-SLC31A1-...

MeSH Terms: Cation Transport Proteins, Cloning, Molecular, Copper Transporter 1, Cysteine, Dimerization, Electrophoresis, Polyacrylamide Gel, Humans, Magnetic Resonance Spectroscopy, Models, Biological, Models, Genetic, Protein Folding