2JPD
Solution structure of the ERCC1 central domain
2JPD の概要
| エントリーDOI | 10.2210/pdb2jpd/pdb |
| NMR情報 | BMRB: 15240 |
| 分子名称 | DNA excision repair protein ERCC-1 (1 entity in total) |
| 機能のキーワード | protein, dna binding protein |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15461.83 |
| 構造登録者 | Tripsianes, K.,Folkers, G.,Zheng, C.,Das, D.,Grinstead, J.S.,Kaptein, R.,Boelens, R. (登録日: 2007-05-06, 公開日: 2007-09-04, 最終更新日: 2024-05-08) |
| 主引用文献 | Tripsianes, K.,Folkers, G.E.,Zheng, C.,Das, D.,Grinstead, J.S.,Kaptein, R.,Boelens, R. Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization Nucleic Acids Res., 35:5789-5798, 2007 Cited by PubMed Abstract: Human ERCC1/XPF is a structure-specific endonuclease involved in multiple DNA repair pathways. We present the solution structure of the non-catalytic ERCC1 central domain. Although this domain shows structural homology with the catalytically active XPF nuclease domain, functional investigation reveals a completely distinct function for the ERCC1 central domain by performing interactions with both XPA and single-stranded DNA. These interactions are non-competitive and can occur simultaneously through distinct interaction surfaces. Interestingly, the XPA binding by ERCC1 and the catalytic function of XPF are dependent on a structurally homologous region of the two proteins. Although these regions are strictly conserved in each protein family, amino acid composition and surface characteristics are distinct. We discuss the possibility that after XPF gene duplication, the redundant ERCC1 central domain acquired novel functions, thereby increasing the fidelity of eukaryotic DNA repair. PubMed: 17720715DOI: 10.1093/nar/gkm503 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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