1HKS
SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR
1HKS の概要
| エントリーDOI | 10.2210/pdb1hks/pdb |
| 分子名称 | HEAT-SHOCK TRANSCRIPTION FACTOR (1 entity in total) |
| 機能のキーワード | transcription regulation |
| 由来する生物種 | Drosophila melanogaster (fruit fly) |
| 細胞内の位置 | Nucleus: P22813 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12409.18 |
| 構造登録者 | Vuister, G.W.,Kim, S.-J.,Orosz, A.,Marquardt, J.L.,Wu, C.,Bax, A. (登録日: 1994-07-18, 公開日: 1994-09-30, 最終更新日: 2024-05-22) |
| 主引用文献 | Vuister, G.W.,Kim, S.J.,Orosz, A.,Marquardt, J.,Wu, C.,Bax, A. Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nat.Struct.Biol., 1:605-614, 1994 Cited by PubMed Abstract: The solution structure of the DNA-binding domain of the Drosophila heat shock transcription factor, as determined by multidimensional multinuclear NMR, resembles that of the helix-turn-helix class of DNA-binding proteins. The domain comprises a four-stranded antiparallel beta-sheet, packed against a three-helix bundle. The second helix is significantly distorted and is separated from the third helix by an extended turn which is subject to conformational averaging on an intermediate time scale. Helix 3 forms a classical amphipathic helix with polar and charged residues exposed to the solvent. Upon titration with DNA, resonance shifts in the backbone and Asn and Gln side-chain amides indicate that helix 3 acts as the recognition helix of the heat shock transcription factor. PubMed: 7634100DOI: 10.1038/nsb0994-605 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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