1PET
NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53
1PET の概要
| エントリーDOI | 10.2210/pdb1pet/pdb |
| 分子名称 | TUMOR SUPPRESSOR P53 (1 entity in total) |
| 機能のキーワード | dna-binding |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 15064.89 |
| 構造登録者 | Lee, W.,Harvey, T.S.,Yin, Y.,Yau, P.,Litchfield, D.,Arrowsmith, C.H. (登録日: 1994-11-24, 公開日: 1995-02-07, 最終更新日: 2024-05-22) |
| 主引用文献 | Lee, W.,Harvey, T.S.,Yin, Y.,Yau, P.,Litchfield, D.,Arrowsmith, C.H. Solution structure of the tetrameric minimum transforming domain of p53. Nat.Struct.Biol., 1:877-890, 1994 Cited by PubMed Abstract: We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA. PubMed: 7773777DOI: 10.1038/nsb1294-877 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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