3R45
Structure of a CENP-A-Histone H4 Heterodimer in complex with chaperone HJURP
3R45 の概要
エントリーDOI | 10.2210/pdb3r45/pdb |
分子名称 | Histone H3-like centromeric protein A, Histone H4, Holliday junction recognition protein, ... (6 entities in total) |
機能のキーワード | histone fold, centromere, cenp-a, histone chaperone, hjurp, nuclear protein |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Nucleus: P49450 P62805 Nucleus, nucleolus: Q8NCD3 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 40400.03 |
構造登録者 | |
主引用文献 | Hu, H.,Liu, Y.,Wang, M.,Fang, J.,Huang, H.,Yang, N.,Li, Y.,Wang, J.,Yao, X.,Shi, Y.,Li, G.,Xu, R.M. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP Genes Dev., 25:901-906, 2011 Cited by PubMed Abstract: In higher eukaryotes, the centromere is epigenetically specified by the histone H3 variant Centromere Protein-A (CENP-A). Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer. The C-terminal β-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing it from spontaneous association with DNA. Our analysis also revealed a novel site in CENP-A that distinguishes it from histone H3 in its ability to bind HJURP. These findings provide key information for specific recognition of CENP-A and mechanistic insights into the process of centromeric chromatin assembly. PubMed: 21478274DOI: 10.1101/gad.2045111 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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