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Biochim Biophys Acta. 2007 Dec;1768(12):3127-34. Epub 2007 Sep 21.

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

Author information

1
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

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.

PMID:
17959139
PMCID:
PMC2275670
DOI:
10.1016/j.bbamem.2007.08.037
[Indexed for MEDLINE]
Free PMC Article

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