Tertiary structure of transcriptional co-activators.
| Project/Area Number |
09680652
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
SHIRAKAWA Masahiro Nara Institute of Science and Technology, Assistant Professor, バイオサイエンス研究科, 助教授 (00202119)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 1998: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1997: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | tertiary structure / transcription factor / NMR / Protein / protein-protein interaction / DNA binding protein / DNA結合蛋白質 / 遺伝子転写 / 蛋白質-蛋白質相互作用 |
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| Research Abstract |
Bombyx mori and human MBFl
Tertiary structures of the core domains of Born byx mori and human MBFI were determined by means of multi-dimensional multi-nuclear NMR.The core domains are capable of binding to TBP.Both of them consists of four a helices and the connecting loops. By mutation analyses, residues indispensable for the transactivations have been identified.
The central domain of human repair factor XPA
The solution structure of the central domain of the human nucleotide excision repair (NER) protein XPA, which is responsible for the binding to damaged DNA and replication protein A (RPA), was determined by NMR spectroscopy. The central domain consists of a zinc-containing subdomain and a carboxyl-terminal subdomain. The zinc-containing subdomain has a compact globular structure and is distinct from the zinc-fingers found in transcription factors. The carboxyl-terminal subdomain folds into a novel alpha / beta structure with a positively charged superficial cleft, From the NMR spectra of the complexes, DNA and RPA binding surfaces are suggested.
The complex of hDLG PDZ domain between the C-terminal of APC
Tertiary structure of the complex between the PDZ2 domain of human tumor suppressor hDLG and the C-terminal peptide was determined by multi-dimensional multi-nuclear NMR.The PDZ2 folds into an a /beta structure with a cleft formed between a beta sheet and an a helix. The bound C-terminal peptide of APC was found to be located in the cleft, making hydrophobic and electric interactions with the PDZ2 domain.
F.coli ArcB
Structure of the phosphotransfer domain of E.ccli sensor kinase ArcB was determined by multi-dimensional multi-nuclear NMR.It folds into an a structure with five helices. Analyses of the dynamic properties of the domain by means of measuring 15N relaxation rates revealed that the are that contains the active histidine exhibited a characteristic dynamic property.
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Report
(3 results)
Research Products
(10 results)
