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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1998-2-4
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pubmed:databankReference |
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pubmed:abstractText |
Menkes disease is an X-linked disorder in copper transport that results in death during early childhood. The solution structures of both apo and Ag(I)-bound forms of the fourth metal-binding domain (mbd4) from the Menkes copper-transporting ATPase have been solved. The 72-residue mbd4 has a ferredoxin-like beta alpha beta beta alpha beta fold. Structural differences between the two forms are limited to the metal-binding loop, which is disordered in the apo structure but well ordered in the Ag(I)-bound structure. Ag(I) binds in a linear bicoordinate manner to the two Cys residues of the conserved GMTCxxC motif; Cu(I) likely coordinates in a similar manner. Menkes mbd4 is thus the first bicoordinate copper-binding protein to be characterized structurally. Sequence comparisons with other heavy-metal-binding domains reveal a conserved hydrophobic core and metal-binding motif.
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pubmed:commentsCorrections |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/ATP7A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metals, Heavy,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9437429-Adenosine Triphosphatases,
pubmed-meshheading:9437429-Amino Acid Sequence,
pubmed-meshheading:9437429-Apoproteins,
pubmed-meshheading:9437429-Binding Sites,
pubmed-meshheading:9437429-Carrier Proteins,
pubmed-meshheading:9437429-Cation Transport Proteins,
pubmed-meshheading:9437429-Copper,
pubmed-meshheading:9437429-Cysteine,
pubmed-meshheading:9437429-Humans,
pubmed-meshheading:9437429-Membrane Proteins,
pubmed-meshheading:9437429-Metals, Heavy,
pubmed-meshheading:9437429-Molecular Sequence Data,
pubmed-meshheading:9437429-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9437429-Protein Structure, Secondary,
pubmed-meshheading:9437429-Protein Structure, Tertiary,
pubmed-meshheading:9437429-Recombinant Fusion Proteins,
pubmed-meshheading:9437429-Recombinant Proteins,
pubmed-meshheading:9437429-Sequence Alignment,
pubmed-meshheading:9437429-Sequence Homology, Amino Acid,
pubmed-meshheading:9437429-Solutions,
pubmed-meshheading:9437429-Structure-Activity Relationship
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pubmed:year |
1998
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pubmed:articleTitle |
Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.
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pubmed:affiliation |
Howard Hughes Medical Institute, University of California, San Francisco 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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