Electronic Reprint Biological Crystallography Structure of the Taz2 Domain of P300: Insights into Ligand Binding Biological Crystallography Structure of the Taz2 Domain of P300: Insights into Ligand Binding
Electronic Reprint Biological Crystallography Structure of the Taz2 Domain of P300: Insights into Ligand Binding Biological Crystallography Structure of the Taz2 Domain of P300: Insights into Ligand Binding
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通讯作者：
Maria Miller;Z. Dauter;S. Cherry;J. Tropea;A. Wlodawer
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作者：
Maria Miller;Z. Dauter;S. Cherry;J. Tropea;A. Wlodawer
本文作者可在保留本封面页的前提下，将转载本文件载入自己的网站或机构资料库。未经IUCr事先书面许可，不得转载本文或将其存储在电子数据库中。晶体学学报D部分：生物晶体学欢迎提交涵盖结构生物学任何方面的论文，特别强调生物大分子的结构及其测定方法。特别鼓励关于新蛋白质结构的报告，以及结构-功能论文，其中可能包括晶体学结合研究，或突变体或已知蛋白质结构的其他修饰形式的结构分析。关键的标准是，这些论文应该提出对生物学、化学或结构的新见解。关于晶体学方法的论文应该面向生物晶体学，并且可以包括结构确定或分析的任何方面的新方法。CBP及其同源蛋白p300是组蛋白乙酰基转移酶，通过与多个转录因子通过专门的结构域相互作用来调节基因表达。研究了人p300蛋白的一个区段（残基1723-1836）的结构，该区段对应于延伸的锌结合Taz 2结构域。利用结合Zn离子的异常衍射信号，通过SAD方法求解晶体结构。该结构包括由三个锌离子稳定的非典型螺旋束，并且与之前针对较短肽确定的溶液结构非常相似。来自当前构建体的残基1813-1834形成C-末端螺旋的螺旋延伸，并与Taz 2的肽结合位点进行广泛的晶体接触相互作用，为Taz 2识别不同的反式激活结构域（TADs）的机制提供了额外的见解。基于这些结果和分子模拟，提出了磷酸化p53 TAD 1与Taz 2结合的假设模型。PDB参考：p300、3 io 2、r3 io 2sf的Taz 2结构域。
Author(s) of this paper may load this reprint on their own web site or institutional repository provided that this cover page is retained. Republication of this article or its storage in electronic databases other than as specified above is not permitted without prior permission in writing from the IUCr. Acta Crystallographica Section D: Biological Crystallography welcomes the submission of papers covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules and the methods used to determine them. Reports on new protein structures are particularly encouraged, as are structure–function papers that could include crystallographic binding studies, or structural analysis of mutants or other modified forms of a known protein structure. The key criterion is that such papers should present new insights into biology, chemistry or structure. Papers on crystallographic methods should be oriented towards biological crystallography, and may include new approaches to any aspect of structure determination or analysis. CBP and its paralog p300 are histone acetyl transferases that regulate gene expression by interacting with multiple transcription factors via specialized domains. The structure of a segment of human p300 protein (residues 1723–1836) corresponding to the extended zinc-binding Taz2 domain has been investigated. The crystal structure was solved by the SAD approach utilizing the anomalous diffraction signal of the bound Zn ions. The structure comprises an atypical helical bundle stabilized by three Zn ions and closely resembles the solution structures determined previously for shorter peptides. Residues 1813–1834 from the current construct form a helical extension of the C-terminal helix and make extensive crystal-contact interactions with the peptide-binding site of Taz2, providing additional insights into the mechanism of the recognition of diverse transactivation domains (TADs) by Taz2. On the basis of these results and molecular modeling, a hypothetical model of the binding of phosphorylated p53 TAD1 to Taz2 has been proposed. PDB Reference: Taz2 domain of p300, 3io2, r3io2sf.