SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53
SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53
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DOI：
10.1038/nsb1294-877
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发表时间：
1994-12-01
期刊：
影响因子：
--
通讯作者：
ARROWSMITH, CH
中科院分区：
文献类型：
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作者：
LEE, WT;HARVEY, TS;ARROWSMITH, CH
我们报告的解决方案结构的最小转换域（残基303-366）的人p53（p53 tet）的多维NMR光谱测定。该结构域包含许多与p53活性相关的重要功能，包括转化、寡聚化、核定位和p34/cdc 2激酶的磷酸化位点。p53 tet形成二聚体的对称二聚体，其与最近报道的该结构域的较短构建体的结构显著不同。Ser 315的磷酸化仅具有较小的结构后果，因为蛋白质的该区域是非结构化的。基于p53 tet结构的建模表明全长p53中相邻结构域之间的相互作用以及与DNA相互作用的模式可能是模式。
We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.