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.

BOMBYX MORI和人类Mbfltertiary结构由Byx Mori和人类MBFI的核心结构域通过多维多核NMR确定。核心结构域能够与TBP结合。它们由四个A螺旋螺旋和连接回路组成。通过突变分析，已经确定了反式激活必不可少的残基。人修复因子XPathe X Pathe溶液解决方案的中心结构域的中心结构域的中心结构域的结构是通过NMR光谱确定与受损的DNA和重复蛋白A（RPA）结合的，该蛋白XPA XPA XPA，该蛋白XPA的结构。中心域由含锌的亚域和羧基末端亚域组成。含锌的亚域具有紧凑的球状结构，与转录因子中发现的锌膜不同。羧基末端亚域折叠成一个新型的α /β结构，并提出了带有带正电荷的表面裂解的，提出了复合物，DNA和RPA结合表面的NMR光谱，HDLG PDZ结构域的复合物的复合物之间的复合物在pdz2 domart and pdem pdem的C-末端之间的c-末端pdz2 domern themorn themor themor themor thumor themor themor thumor themorn themor perters thum thumorn themor perters humon primest humon prime thum tumor thum thum thumore p.由多维多核NMR确定。PDZ2折叠成A /beta结构，在β板和A螺旋之间形成裂缝。发现APC的结合C末端肽位于裂缝中，使E.CCLI传感器激酶ARCB的磷酸转移域的疏水和电相互作用由多维多维多核电型NMR.It nmr.it folds a A A ARCBS确定。通过测量15N弛豫率对域的动态特性的分析表明，其中包含活性组氨酸的是表现出特征性的动态特性。