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Structure of the Taz2 domain of p300: Insights into ligand binding

机译:p300 Taz2结构域:见解在配体结合

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摘要

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.
机译:海关与边境保护局及其假字p300是组蛋白乙酰基转移酶,调节基因的表达与多个转录因子相互作用通过专门的领域。部分人类p300的蛋白质(残留物1723 - 1836年)的扩展锌结合Taz2域被调查。的晶体结构解决了悲伤方法利用反常衍射绑定锌离子的信号。包括非典型螺旋束稳定由三个锌离子和相似解决方案结构决定之前短肽。当前构建形成一个螺旋形的延伸c端螺旋和广泛crystal-contact交互的Taz2 peptide-binding网站,提供额外的洞察的机制识别不同的transactivation域(由Taz2 TADs)。分子建模的假设模型绑定的磷酸化p53 TAD1 Taz2被提出。

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