生物大分子结构与功能第10章真核生物转录因子的dna识别.pptVIP

Different Views of p53 Tetramers Bound to DNA. Four p53 core domains (designated as A, B, C, and D) shown in ribbon representation interact with two double-stranded DNA half-sites. The core tetramer is a dimer of dimers: A-B (in cyan) and C-D (in green). The four Zn ions are shown as magenta spheres. 图10-22 p53蛋白中最易发生致肿瘤突变的三个结构区域 第十章 真核生物转录因子的DNA识别 图10-1 一段DNA大区域上的真核结构基因的转录单元 图10-2 转录激活的模型 图10-3 TATA Box与复合物晶体结构中的DNA顺序 图10-4 TATA Box 结合蛋白（TBP）的结构 图10-5 TBP蛋白和含有TATA Box DNA片段复合 物的结构 图10-6 DNA片段在TATA Box 区域产生了严重的弯曲 图10-7 TBP 蛋白和TATA Box之间的专一性相互作用 TBP-TFIIB-TATA Box Complex NC2 binding precludes recruitment of TFIIB and TFIIA to a preformed TBP-DNA complex. Molecular surface representations of NC2 (blue mesh), TFIIB (solid gray), and TFIIA (red mesh) bound to TBP (green) and DNA (yellow/orange ribbons). TFIIA-TFIIB-TBP-DNA Complex (A) modification of K97C TBP with the affinity cleavage reagent IAAOP to produce K97C-OP and (B) the regions of the promoter that are expected to be cleaved, as indicated by the gray arrows. Molecular model of the quaternary K97C-TFIIB-TFIIA-TATA complex generated on the basis of ternary complex crystal structures. 图10-8 Antennapedia homeodomain的结构 图10-9 Homeodomain的螺旋-转折-螺旋花样与? repressor的相同花样的比较 图10-10 DNA和一个单体的hemeodomain的相互作用 图10-11 四种不同转录因子的homeodomain的氨基酸顺序比较 图10-12 酵母转录因子Mat ?2-Mat a1与DNA结合的异二体的结构 图10-13 与DNA结合的Oct-1蛋白的POU区域 图10-14 POU区域的两个结构域一前一后地在相反 的方向上结合在DNA双螺旋上 Structure of the ternary complex of the OCA-B1–44 peptide, the Oct-1 POU domain, and an octamer element. Overview of the ternary complex showing the OCA-B peptide (purple), the Oct-1 POU domain (the POU homeodomain is in red; the POU specific domain is in yellow), and DNA containing the octamer sequence (position 5 is in green). About 20 amino acids of the OCA-B 1–44 peptide are well-ordered in the crystal. 图10-15 DNA与POU区域间的顺序专一性相互作用 图10-16 p53蛋