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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2005-12-12
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pubmed:abstractText |
We describe a structural model for DNA binding by the caspase-activated DNase (CAD). Results of a mutational analysis and computational modeling suggest that DNA is bound via a positively charged surface with two functionally distinct regions, one being the active site facing the DNA minor groove and the other comprising distal residues close to or directly from helix alpha4, which binds DNA in the major groove. This bipartite protein-DNA interaction is present once in the CAD/inhibitor of CAD heterodimer and repeated twice in the active CAD dimer.
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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 |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41707-15
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16236713-Amino Acid Sequence,
pubmed-meshheading:16236713-Animals,
pubmed-meshheading:16236713-Arginine,
pubmed-meshheading:16236713-Binding Sites,
pubmed-meshheading:16236713-Crystallography, X-Ray,
pubmed-meshheading:16236713-DNA,
pubmed-meshheading:16236713-DNA Mutational Analysis,
pubmed-meshheading:16236713-Deoxyribonucleases,
pubmed-meshheading:16236713-Dimerization,
pubmed-meshheading:16236713-Dose-Response Relationship, Drug,
pubmed-meshheading:16236713-Escherichia coli,
pubmed-meshheading:16236713-Genetic Variation,
pubmed-meshheading:16236713-Glutathione Transferase,
pubmed-meshheading:16236713-Humans,
pubmed-meshheading:16236713-Models, Molecular,
pubmed-meshheading:16236713-Molecular Sequence Data,
pubmed-meshheading:16236713-Phenylalanine,
pubmed-meshheading:16236713-Poly Adenosine Diphosphate Ribose,
pubmed-meshheading:16236713-Protein Binding,
pubmed-meshheading:16236713-Protein Conformation,
pubmed-meshheading:16236713-Protein Structure, Tertiary,
pubmed-meshheading:16236713-Recombinant Proteins,
pubmed-meshheading:16236713-Sequence Homology, Amino Acid
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pubmed:year |
2005
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pubmed:articleTitle |
Structural basis for stable DNA complex formation by the caspase-activated DNase.
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pubmed:affiliation |
Institute of Biochemistry, Faculty of Biology and Chemistry, Justus-Liebig-University Giessen, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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