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Tertiary structure of transcriptional co-activators.

转录共激活子的三级结构。

基本信息

批准号：
09680652
负责人：
SHIRAKAWA Masahiro
金额：
$ 2.05万
依托单位：
Nara Institute of Science and Technology
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
1997
资助国家：
日本
起止时间：
1997 至 1998
项目状态：
已结题

项目摘要

Bombyx mori and human MBFlTertiary 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 XPAThe 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 APCTertiary 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 ArcBStructure 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.

用多维多核核磁共振方法测定了家蚕和人MBFI核心区的三级结构。核心区能与TBP结合，它们都由四个a螺旋和连接环组成。通过突变分析，确定了反式激活所必需的残基。用核磁共振波谱测定了人修复因子XPA的中心结构域，该结构域是人核苷酸切除修复(NER)蛋白XPA的中心结构域，负责与受损的DNA和复制蛋白A(RPA)结合。中心结构域由一个含锌亚域和一个羧基末端亚域组成。含锌亚结构域具有紧密的球状结构，与转录因子中发现的锌指不同。通过多维多核核磁共振确定了hDLG PDZ结构域的C-末端与C-末端多肽之间的复合体。PDZ2折叠成a/β结构，在β-折叠和螺旋之间形成裂隙。APC结合的C-端肽位于裂隙中，与PDZ2结构域发生疏水和电性相互作用。E.ColiArcB通过多维多核核磁共振确定E.ccli传感器激酶ArcB的磷酸转移结构域的结构，折叠成五个螺旋的a结构。通过测量15N驰豫速率对结构域的动力学性质进行了分析，发现含有活性组氨酸的ARE具有特征的动力学性质。