Crystal structure of a p53 core tetramer bound to DNA.
Crystal structure of a p53 core tetramer bound to DNA.
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DOI:
10.1038/onc.2008.400
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发表时间:
2009-01-22
期刊:
影响因子:
8
通讯作者:
Marmorstein, R.
中科院分区:
文献类型:
--
作者:
Malecka, K. A.;Ho, W. C.;Marmorstein, R.
The tumor suppressor p53 regulates downstream genes in response to many cellular stresses and is frequently mutated in human cancers. Here, we report the use of a crosslinking strategy to trap a tetrameric p53 DNA binding domain (p53DBD) bound to DNA and the X-ray crystal structure of the protein/DNA complex. The structure reveals that two p53DBD dimers bind to B form DNA with no relative twist and that a p53 tetramer can bind to DNA without introducing significant DNA bending. The numerous dimer-dimer interactions involve several strictly conserved residues thus suggesting a molecular basis for p53DBD-DNA binding cooperativity. Surface residue conservation of the p53DBD tetramer bound to DNA highlights possible regions of other p53 domain or p53 cofactor interactions.
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影响因子:
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作者:
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通讯作者:
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DOI:
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
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通讯作者:
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