1BF5
TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX
1BF5 の概要
| エントリーDOI | 10.2210/pdb1bf5/pdb |
| 分子名称 | DNA (5'-D(*AP*CP*AP*GP*TP*TP*TP*CP*CP*CP*GP*TP*AP*AP*AP*TP*G P*C)-3'), DNA (5'-D(*TP*GP*CP*AP*TP*TP*TP*AP*CP*GP*GP*GP*AP*AP*AP*CP*T P*G)-3'), SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 1-ALPHA/BETA (3 entities in total) |
| 機能のキーワード | complex (sh2 domain-dna), sh2 domain, transcription factor, gene regulation-dna complex, gene regulation/dna |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cytoplasm : P42224 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 77688.49 |
| 構造登録者 | Kuriyan, J.,Zhao, Y.,Chen, X.,Vinkemeier, U.,Jeruzalmi, D.,Darnell Jr., J.E. (登録日: 1998-05-27, 公開日: 1998-08-12, 最終更新日: 2024-11-20) |
| 主引用文献 | Chen, X.,Vinkemeier, U.,Zhao, Y.,Jeruzalmi, D.,Darnell Jr., J.E.,Kuriyan, J. Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell(Cambridge,Mass.), 93:827-839, 1998 Cited by PubMed Abstract: The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements. PubMed: 9630226DOI: 10.1016/S0092-8674(00)81443-9 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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