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rdf:type |
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lifeskim:mentions |
umls-concept:C0024485,
umls-concept:C0079866,
umls-concept:C0086418,
umls-concept:C0185026,
umls-concept:C0251220,
umls-concept:C0376525,
umls-concept:C0719517,
umls-concept:C1420182,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C2349182
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pubmed:issue |
12
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pubmed:dateCreated |
2007-12-17
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-10820006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-10940336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-11276254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-11395420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-11734551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12034741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12039007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12042066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12079778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12357033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12370430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12391279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-12466020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-15099070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-15303829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-15385536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-15607932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-15634665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-16043693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-16135512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-16501047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-16569016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-16847145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-17211682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-1925542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-8293472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-8756349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-8757792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-9207117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17959139-9818271
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1768
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3127-34
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:17959139-Cation Transport Proteins,
pubmed-meshheading:17959139-Cloning, Molecular,
pubmed-meshheading:17959139-Cysteine,
pubmed-meshheading:17959139-Dimerization,
pubmed-meshheading:17959139-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:17959139-Humans,
pubmed-meshheading:17959139-Magnetic Resonance Spectroscopy,
pubmed-meshheading:17959139-Models, Biological,
pubmed-meshheading:17959139-Models, Genetic,
pubmed-meshheading:17959139-Protein Folding
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pubmed:year |
2007
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pubmed:articleTitle |
NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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