Tertiary structure of transcriptional co-activators.

家蚕和人MBFI核心结构域的三级结构采用多维多核磁共振法测定。核心结构域能够与TBP结合。它们都由四个a螺旋和连接环组成。通过突变分析，已经确定了交易所必需的残基。人类核苷酸切除修复（NER）蛋白XPA中心结构域的溶液结构通过核磁共振光谱测定了其与受损DNA和复制蛋白A （RPA）的结合。中心结构域由一个含锌子结构域和一个羧基末端子结构域组成。含锌亚结构域具有致密的球状结构，与转录因子中的锌指结构不同。羧基末端亚结构域折叠成具有带正电的表面裂缝的新型α / β结构，从配合物的核磁共振光谱可以推测出DNA和RPA的结合面。通过多维多核核磁共振测定了hDLG在apc端PDZ结构域之间的配合物，以及hDLG PDZ2结构域与c端肽之间的配合物的三级结构。PDZ2折叠成a / β结构，在β薄片和a螺旋之间形成裂缝。发现APC的结合c端肽位于裂缝中，与PDZ2结构域发生疏水和电相互作用。f.c oli ArcB通过多维多核磁共振测定了e.c i传感器激酶ArcB的磷酸转移结构域结构。它折叠成一个有五个螺旋的结构。通过测量15N弛豫率对结构域的动态特性进行了分析，发现含有活性组氨酸的结构域具有典型的动态特性。

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.