3X1S

Crystal structure of the nucleosome core particle

3X1S の概要

• エントリーDOI: 10.2210/pdb3x1s/pdb
• 関連するPDBエントリー: 3X1T 3X1U 3X1V
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total)
• 機能のキーワード: histones, nuclosome core particle, structural protein-dna complex, structural protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P68431 P62805 P04908 P33778
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 199415.50

構造登録者

Sivaraman, P.,Kumarevel, T.S. (登録日: 2014-11-27, 公開日: 2015-09-23, 最終更新日: 2023-11-08)

主引用文献

Padavattan, S.,Shinagawa, T.,Hasegawa, K.,Kumasaka, T.,Ishii, S.,Kumarevel, T.
Structural and functional analyses of nucleosome complexes with mouse histone variants TH2a and TH2b, involved in reprogramming
Biochem.Biophys.Res.Commun., 464:929-935, 2015

PubMed Abstract: Histone variants TH2a and TH2b are highly expressed in testes, oocytes and zygotes. Our recent analysis suggested that these histone variants enhance the induced generation of pluripotent stem cells (iPSCs) when co-expressed along with four transcription factors, Oct3/4, Sox2, Klf4 and c-Myc (OSKM), and are associated with an open chromatin structure [1]. In the present study, we report the crystal structures of nucleosomes (NCPs) with the mouse histone variants, TH2a and TH2b. The structures revealed two significant changes, as compared to the canonical counterparts: fewer histone-DNA contacts and changes in dimer-dimer interactions between TH2a-TH2a' (L1-loop). In vivo studies with domain swapping and point mutants of the variants revealed that the residues in the histone tails and the TH2a-L1 loop are important for reprogramming. Taken together, our work indicates that the NCP variants with structural modifications and flexible tails are most likely important for enhanced reprogramming of functions.

PubMed: 26188507
DOI: 10.1016/j.bbrc.2015.07.070

実験手法

X-RAY DIFFRACTION (2.805 Å)