1C26
CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN
1C26 の概要
| エントリーDOI | 10.2210/pdb1c26/pdb |
| 分子名称 | P53 TUMOR SUPPRESSOR (2 entities in total) |
| 機能のキーワード | tetramer, gene regulation |
| 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 | 1 |
| 化学式量合計 | 3823.27 |
| 構造登録者 | |
| 主引用文献 | Jeffrey, P.D.,Gorina, S.,Pavletich, N.P. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science, 267:1498-1502, 1995 Cited by PubMed Abstract: The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a beta strand and an alpha helix, associates with a second monomer across an antiparallel beta sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer. PubMed: 7878469主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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