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| http://purl.uniprot.org/citations/17959139 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/17959139 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamem.2007.08.037"xsd:string |
| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/author | "Lee S."xsd:string |
| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/author | "Opella S.J."xsd:string |
| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/author | "Howell S.B."xsd:string |
| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
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| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/title | "NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization."xsd:string |
| http://purl.uniprot.org/citations/17959139 | http://purl.uniprot.org/core/volume | "1768"xsd:string |
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