Crystal structure of the nucleosome core particle at 2.8 angstrom resolution
Crystal structure of the nucleosome core particle at 2.8 angstrom resolution
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DOI：
10.1038/38444
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发表时间：
1997-09-18
期刊：
影响因子：
64.8
通讯作者：
Richmond, TJ
中科院分区：
文献类型：
--
作者：
Luger, K;Mader, AW;Richmond, TJ
染色质的核小体空洞颗粒的X射线晶体结构以原子细节展示了组蛋白八聚体是如何组装的，以及146个碱基对的DNA是如何组织成它周围的超螺旋的。组蛋白/组蛋白和组蛋白/DNA的相互作用都依赖于组蛋白折叠结构域和从这个基序延伸出来的额外的、有序的结构元件。组蛋白氨基末端的尾巴穿过DNA超螺旋的环状结构并在环间传递，以接触邻近的颗粒。多个组蛋白/DNA结合位点之间缺乏一致性导致DNA偏离理想的超螺旋几何形状。
The X-ray crystal structure of the nucleosome cave particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The lack of uniformity between multiple histone/DNA-binding sites causes the DNA to deviate from ideal superhelix geometry.