CRYSTAL-STRUCTURE OF GLOBULAR DOMAIN OF HISTONE H5 AND ITS IMPLICATIONS FOR NUCLEOSOME BINDING

被引：660

作者：

RAMAKRISHNAN, V ^{[1
]}

FINCH, JT ^{[1
]}

GRAZIANO, V ^{[1
]}

LEE, PL ^{[1
]}

SWEET, RM ^{[1
]}

机构：

[1] MRC,MOLEC BIOL LAB,CAMBRIDGE CB2 2QH,ENGLAND

来源：

NATURE | 1993年 / 362卷 / 6417期

关键词：

D O I：

10.1038/362219a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 angstrom 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.

引用

页码：219 / 223

页数：5

共 47 条

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