Source:http://linkedlifedata.com/resource/pubmed/id/15578823
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
25
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| pubmed:dateCreated |
2004-12-6
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| pubmed:abstractText |
The metal binding properties of peptides corresponding to metal-binding sites spanning regions that normally function as linkers in tandem arrays of metal-binding domain-containing proteins were examined. For a peptide with two His residues from one TFIIIA-like zinc finger domain, a canonical TFIIIA-like linker, and two Cys residues from an adjacent zinc domain, the dissociation constant for the 1:1 peptide to cobalt(II) was found to be 15 +/- 10 microM, compared with 60 nM for the corresponding zinc finger domains themselves. Peptides overlapping two sets of metal-binding domains from human TRAF (tumor necrosis factor receptor-associated factor) proteins were examined. In one case, the affinity of the presumed metal-binding domain and that for the linker region were comparable, while in the second case, the affinity of the linker peptide was higher than that for the corresponding presumed metal-binding domain peptide. These studies revealed that cobalt(II) affinities in the micromolar range can occur even for peptides that do not correspond to natural zinc-binding domains and that the degree of distinction between authentic metal-binding domains and the corresponding linker-spanning peptides may be modest, at least for single domain peptide models.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0020-1669
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
13
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| pubmed:volume |
43
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
7897-901
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| pubmed:meshHeading |
pubmed-meshheading:15578823-Amino Acid Sequence,
pubmed-meshheading:15578823-Binding Sites,
pubmed-meshheading:15578823-Metals,
pubmed-meshheading:15578823-Models, Molecular,
pubmed-meshheading:15578823-Molecular Sequence Data,
pubmed-meshheading:15578823-Peptides,
pubmed-meshheading:15578823-Protein Binding,
pubmed-meshheading:15578823-Protein Conformation,
pubmed-meshheading:15578823-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15578823-Transcription Factor TFIIIA,
pubmed-meshheading:15578823-Tumor Necrosis Factor Receptor-Associated Peptides and...,
pubmed-meshheading:15578823-Zinc Fingers
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| pubmed:year |
2004
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| pubmed:articleTitle |
Site selection in tandem arrays of metal-binding domains.
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| pubmed:affiliation |
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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| pubmed:publicationType |
Journal Article
|