Structural characterization of histone H2A variants
Structural characterization of histone H2A variants
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DOI：
10.1101/sqb.2004.69.227
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发表时间：
2004-01-01
期刊：
影响因子：
--
通讯作者：
Luger, K
中科院分区：
文献类型：
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作者：
Chakravarthy, S;Bao, Y;Luger, K
图1所示。组蛋白H2A变体。(A)核小体结构概述。只有74个碱基对的DNA和相关蛋白质被显示出来。黄色:H2A;红色:H2B;蓝色:H3;格林:H4。非晶体对称的轴用虚线表示。由两个H3分子和H2A对接域形成的四螺旋束结构被框起来；还指出了其他结构特征。(B)人H2A组蛋白结构域序列比对。X，鼠标H2A。Z，小鼠macroH2A，人类H2A。大鼠H2A。子弹：大H2A中每10个残留物；黑色：相同残留物；蓝色：相似残留物；红色：不同的残数。组蛋白折叠的二级结构元素（α1、α2和α3）以及环和延伸（L1、L2、αN和αC）也被标记出来。
Figure 1. Histone H2A variants.(A) Overview of nucleosome structure. Only 74 base pairs of DNA and associated proteins are shown. Yellow: H2A; red: H2B; blue: H3; green: H4. The axis of noncrystallographic symmetry is indicated by a dashed line. The four-helix bundle structure formed by the two H3 molecules and the H2A docking domain are boxed; other structural features are indicated.(B) Sequence alignment of the histone domain of human H2A. X, mouse H2A. Z, mouse macroH2A, and human H2A. Bbd with majortype mouse H2A. Bullets: every tenth residue in major H2A; black: identical residues; blue: similar residues; red: different residues. Also indicated are the secondary structure elements of the histone fold (α1, α2, and α3) and the loops and extensions (L1, L2, αN, and αC).