Tryptophan scanning analysis of the membrane domain of CTR-copper transporters.

ABSTRACT: Membrane proteins of the CTR family mediate cellular copper uptake in all eukaryotic cells and have been shown to participate in uptake of platinum-based anticancer drugs. Despite their importance for life and the clinical treatment of malignancies, directed biochemical studies of CTR proteins have been difficult because high-resolution structural information is missing. Building on our recent 7A structure of the human copper transporter hCTR1, we present the results of an extensive tryptophan-scanning analysis of hCTR1 and its distant relative, yeast CTR3. The comparative analysis supports our previous assignment of the transmembrane helices and shows that most functionally and structurally important residues are clustered around the threefold axis of CTR trimers or engage in helix packin

SUBMITTER: De Feo CJ 

PROVIDER: S-EPMC2848729 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature