生物大分子结构与功能特殊转录因子.ppt

第十一章 特殊转录因子,图11-1 经典锌指花样和结构,图11-2 Zif 268蛋白DNA结合部位的氨基酸顺序及与Zif 268结合的DNA片段的核苷酸顺序,图11-3 三个Zif 268锌指与DNA结合的复合物结构,Structure of the six-finger TFIIIA–DNA complex.,A model for the nine-finger TFIIIA–DNA complex.,图11-4 Zif 268的第二个锌指与DNA的相互作用,图11-5 六种不同的锌指与DNA顺序专一性结合的比较,a, Secondary structure of 5S RNA 61n, the truncated RNA. Loops A and E are circled and helices are indicated by roman numerals. Sequence of the central three-finger peptide from TFIIIA.,锌指－RNA复合物,b, Some helical positions are indicated. Conserved residues are circled. c, Portion of the electron density map. The RNA is shown as a ball-and-stick model, and finger 5 as a ribbon model.,d, Space-filling model RNA is shown in blue, -sheets in green,  -helices in red, and linkers in purple. The buried surface area is 1,860A2.,Interactions of the three-finger peptide with the RNA. Overall view of the complex of TFIIIA(4–6) and 5S RNA 61n.,图11-6 精氨酸侧链与鸟嘌呤碱基的相互作用,图11-7 进化相关的转录因子受体家族的成员,图11-9 糖皮质激素受体DNA结合结构域的三维结构,图11-10 二体化的糖皮质激素受体与DNA片段复合物的结构,,(A) TheARDBD–ADR3complex. The two protomers are in red and blue, the hexameric half-site DNA is gold, and the spacer and flanking base pairs are black. In brown is a 20-contour of the experimental anomalous Fourier difference map.,(B) The VDR DBD–DR3 complex. VDR DBD protomer A is shown in the same orientation as the AR DBD subunit A in A. The zincs of subunit B fail to occupy the peaks in the anomalous difference Fourier map in this dimeric arrangement, indicating the AR DBD does not form a head-to-tail dimer.,Crystal packing of the AR DBD–ADR3 complex. Red and blue ribbons are the upstream and downstream subunits, respectively.,图11-11 DNA和糖皮质激素受体识别螺旋的顺序专一性相互作用,Interactions of the AR DBD–DNA interfaces. The upstream, cognate, protein–DNA interface. (B) The downstream, noncognate interface. The protein is shown in the same orientation as in A.,图11-12 顺-视黄酸受体与其它核受体形成的异二聚体识别的核苷酸顺序,CAR/RXR Heterodimer Structure in the Complex with CITCO, Fatty Acid, and SRC-1 Peptides. (A) Ribbon diagram of the human CAR/RXR heterodimer complex with two SRC-1 peptides. CITCO is docked in the CAR ligand binding site as described in the text. The SRC-1 peptides are in magenta.,Overall structural architecture of symmetry-related RXR DBD–VDR DBD–DR3 complexes. (A) Ribbon diagram showing two asymmetric crystal units of the complex. (B) Molecular surface representation of the four protomers on two DNA duplexes.,Modeling of the two types of dimerization interfaces which results in homo- and heterocooperative interactions among the DBDs of RXR, RAR and TR.,图11-13 二体化的GAL4转录因子与DNA结合的结构,图11-14 GAL4亚基的DNA结合锌串区域的结构,图11-15 GAL4的一个亚基与DNA结合的结构,图11-16 GAL4蛋白和PPR1蛋白的结构域交换实验,图11-17 转录因子DNA结合结构域28个氨基酸残基区域的螺旋,图11-18 亮氨酸拉链结构的侧链相互作用,图11-19 亮氨酸拉链蛋白的异二聚体化可以改变它们的DNA结合专一性,11-20 转录因子GCN4的DNA结合结构域的氨基酸顺序和晶体结构中所用的DNA片段,图11-21 GCN4的DNA结合结构域的结构,图11-22 GCN4的螺旋碱性区域与DNA片段的顺序专一性相互作用,图11-23 沿真核转录因子b/Zip, b/HLH和b/HLH/Zip三个家族多肽链的排列,图11-24 转录因子MyoD的DNA结合结构域的单体的结构,图11-25 MyoD二体化区域的结构,图11-26 MyoD与DNA结合的结构,图11-27 DNA和MyoD一个单体间的顺序专一性接触,图11-28 转录因子Max与DNA结合的结构,图11-29 Max单体的结构,图11-30 转录因子b/HLH和b/HLH/Zip家族某些成员的HLH区域的氨基酸顺序,图11-31 Max蛋白的一个单体和DNA的顺序专一性相互作用,MyoD蛋白的一个单体和DNA的顺序专一性相互作用,。