组蛋白H5球状结构域的晶体结构及其对核小体结合的影响。
Crystal structure of globular domain of histone H5 and its implications for nucleosome binding.
作者信息
Ramakrishnan V, Finch J T, Graziano V, Lee P L, Sweet R M
机构信息
Biology Department, Brookhaven National Laboratory, Upton, New York 11973.
出版信息
Nature. 1993 Mar 18;362(6417):219-23. doi: 10.1038/362219a0.
DOI:10.1038/362219a0
PMID:8384699
Abstract
The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 A resolution by multiwavelength anomalous diffraction on crystals of the selenomethionyl protein. The structure shows a striking similarity to the DNA-binding domain of the catabolite gene activator protein CAP, thereby providing a possible model for the binding of GH5 to DNA.
摘要
连接组蛋白H5的球状结构域GH5的结构，通过对硒代甲硫氨酸蛋白晶体进行多波长反常衍射，已解析到2.5埃的分辨率。该结构与分解代谢基因激活蛋白CAP的DNA结合结构域有显著相似性，从而为GH5与DNA的结合提供了一个可能的模型。
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