Source:http://linkedlifedata.com/resource/pubmed/id/21471454
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
|
pubmed:dateCreated |
2011-4-27
|
pubmed:databankReference | |
pubmed:abstractText |
The DNA-dependent activator of IFN-regulatory factors (DAI), also known as DLM-1/ZBP1, initiates an innate immune response by binding to foreign DNAs in the cytosol. For full activation of the immune response, three DNA binding domains at the N terminus are required: two Z-DNA binding domains (ZBDs), Z? and Z?, and an adjacent putative B-DNA binding domain. The crystal structure of the Z? domain of human DAI (hZ?(DAI)) in complex with Z-DNA revealed structural features distinct from other known Z-DNA binding proteins, and it was classified as a group II ZBD. To gain structural insights into the DNA binding mechanism of hZ?(DAI), the solution structure of the free hZ?(DAI) was solved, and its bindings to B- and Z-DNAs were analyzed by NMR spectroscopy. Compared to the Z-DNA-bound structure, the conformation of free hZ?(DAI) has notable alterations in the ?3 recognition helix, the "wing," and Y145, which are critical in Z-DNA recognition. Unlike some other Z? domains, hZ?(DAI) appears to have conformational flexibility, and structural adaptation is required for Z-DNA binding. Chemical-shift perturbation experiments revealed that hZ?(DAI) also binds weakly to B-DNA via a different binding mode. The C-terminal domain of DAI is reported to undergo a conformational change on B-DNA binding; thus, it is possible that these changes are correlated. During the innate immune response, hZ?(DAI) is likely to play an active role in binding to DNAs in both B and Z conformations in the recognition of foreign DNAs.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
1091-6490
|
pubmed:author |
pubmed-author:CheongHae-KapHK,
pubmed-author:JeeJungooJ,
pubmed-author:JeonYoung HoYH,
pubmed-author:KangSung WookSW,
pubmed-author:KhayrutdinovBulat IBI,
pubmed-author:KimKyeong KyuKK,
pubmed-author:KimKyungminK,
pubmed-author:KimYang-GyunYG,
pubmed-author:LeeChung-KyungCK,
pubmed-author:LeeSanghoS,
pubmed-author:ParkHyejinH,
pubmed-author:RichAlexanderA
|
pubmed:issnType |
Electronic
|
pubmed:day |
26
|
pubmed:volume |
108
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
6921-6
|
pubmed:dateRevised |
2011-10-26
|
pubmed:meshHeading |
pubmed-meshheading:21471454-DNA, Z-Form,
pubmed-meshheading:21471454-DNA-Binding Proteins,
pubmed-meshheading:21471454-Humans,
pubmed-meshheading:21471454-Immunity, Innate,
pubmed-meshheading:21471454-Models, Molecular,
pubmed-meshheading:21471454-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:21471454-Protein Binding,
pubmed-meshheading:21471454-Protein Structure, Secondary,
pubmed-meshheading:21471454-Protein Structure, Tertiary
|
pubmed:year |
2011
|
pubmed:articleTitle |
Solution structure of the Zbeta domain of human DNA-dependent activator of IFN-regulatory factors and its binding modes to B- and Z-DNAs.
|
pubmed:affiliation |
Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea. kkim@med.skku.ac.kr
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|