1HDD
CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS
1HDD の概要
| エントリーDOI | 10.2210/pdb1hdd/pdb |
| 分子名称 | DNA (5'-D(*TP*TP*TP*TP*GP*CP*CP*AP*TP*GP*TP*AP*AP*TP*TP*AP*C P*CP*TP*AP*A)-3'), DNA (5'-D(*AP*TP*TP*AP*GP*GP*TP*AP*AP*TP*TP*AP*CP*AP*TP*GP*G P*CP*AP*AP*A)-3'), PROTEIN (ENGRAILED HOMEODOMAIN) (3 entities in total) |
| 機能のキーワード | protein-dna complex, double helix, transcription-dna complex, transcription/dna |
| 由来する生物種 | Drosophila melanogaster (fruit fly) 詳細 |
| 細胞内の位置 | Nucleus : P02836 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 27820.51 |
| 構造登録者 | Kissinger, C.R.,Liu, B.,Martin-Blanco, E.,Kornberg, T.B.,Pabo, C.O. (登録日: 1991-09-16, 公開日: 1992-01-15, 最終更新日: 2024-05-22) |
| 主引用文献 | Kissinger, C.R.,Liu, B.S.,Martin-Blanco, E.,Kornberg, T.B.,Pabo, C.O. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions. Cell(Cambridge,Mass.), 63:579-590, 1990 Cited by PubMed Abstract: The crystal structure of a complex containing the engrailed homeodomain and a duplex DNA site has been determined at 2.8 A resolution and refined to a crystallographic R factor of 24.4%. In this complex, two separate regions of the 61 amino acid polypeptide contact a TAAT subsite. An N-terminal arm fits into the minor groove, and the side chains of Arg-3 and Arg-5 make contacts near the 5' end of this "core consensus" binding site. An alpha helix fits into the major groove, and the side chains of IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site. This "recognition helix" is part of a structurally conserved helix-turn-helix unit, but these helices are longer than the corresponding helices in the lambda repressor, and the relationship between the helix-turn-helix unit and the DNA is significantly different. PubMed: 1977522DOI: 10.1016/0092-8674(90)90453-L 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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