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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1993-10-28
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pubmed:abstractText |
Most Cys2His2 zinc finger proteins contain tandem arrays of metal binding domains. The tandem nature of these arrays suggests that metal binding by these domains may not be independent but rather that metal binding may occur in a cooperative manner. This is especially true in light of the crystal structure of a three zinc finger array bound to DNA that revealed several types of interactions between domains. To address this question, peptides containing two tandem domains have been prepared. While metal binding studies do show that the two finger peptide has a metal ion affinity about threefold higher than that for a single domain peptide with the same sequence, additional studies reveal that this behavior is due to increased single site affinities in the context of the two domain peptide rather than to cooperativity. These studies indicate that domains of this type are independent of one another with regard to metal binding, at least in the absence of DNA. This observation has implications with regard to the question of whether the activities of proteins of this class might be modulated by available zinc concentrations.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-1567844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-2028256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-2110530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-2114117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-2248949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-2271546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-2503871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-3047872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-3125980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-3474629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8401216-4040853
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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 |
Aug
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1313-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8401216-Amino Acid Sequence,
pubmed-meshheading:8401216-Binding Sites,
pubmed-meshheading:8401216-CCAAT-Enhancer-Binding Proteins,
pubmed-meshheading:8401216-Cloning, Molecular,
pubmed-meshheading:8401216-DNA-Binding Proteins,
pubmed-meshheading:8401216-Genes, Synthetic,
pubmed-meshheading:8401216-Metals,
pubmed-meshheading:8401216-Molecular Sequence Data,
pubmed-meshheading:8401216-Protein Structure, Secondary,
pubmed-meshheading:8401216-Recombinant Proteins,
pubmed-meshheading:8401216-Transcription Factors,
pubmed-meshheading:8401216-Zinc Fingers
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pubmed:year |
1993
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pubmed:articleTitle |
Independence of metal binding between tandem Cys2His2 zinc finger domains.
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pubmed:affiliation |
Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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