2JSS
NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B
2JSS の概要
エントリーDOI | 10.2210/pdb2jss/pdb |
関連するPDBエントリー | 1YFQ |
NMR情報 | BMRB: 15393 |
分子名称 | Chimera of Histone H2B.1 and Histone H2A.Z, Uncharacterized protein YER030W (2 entities in total) |
機能のキーワード | histone-chaperone complex, intrinsically unfolded protein, chaperone-structural protein complex, chaperone-nuclear protein complex, chaperone/nuclear protein |
由来する生物種 | Saccharomyces cerevisiae (yeast) 詳細 |
細胞内の位置 | Nucleus: Q12692 P40019 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 28033.68 |
構造登録者 | Zhou, Z.,Feng, H.,Hansen, D.F.,Kato, H.,Luk, E.,Freedberg, D.I.,Kay, L.E.,Wu, C.,Bai, Y. (登録日: 2007-07-11, 公開日: 2008-05-20, 最終更新日: 2024-05-29) |
主引用文献 | Zhou, Z.,Feng, H.,Hansen, D.F.,Kato, H.,Luk, E.,Freedberg, D.I.,Kay, L.E.,Wu, C.,Bai, Y. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. Nat.Struct.Mol.Biol., 15:868-869, 2008 Cited by PubMed Abstract: The NMR structure of budding yeast chaperone Chz1 complexed with histones H2A.Z-H2B has been determined. Chz1 forms a long irregular chain capped by two short alpha-helices, and uses both positively and negatively charged residues to stabilize the histone dimer. A molecular model that docks Chz1 onto the nucleosome has implications for its potential functions. PubMed: 18641662DOI: 10.1038/nsmb.1465 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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