1ENH
STRUCTURAL STUDIES OF THE ENGRAILED HOMEODOMAIN
1ENH の概要
| エントリーDOI | 10.2210/pdb1enh/pdb |
| 分子名称 | ENGRAILED HOMEODOMAIN (2 entities in total) |
| 機能のキーワード | dna-binding protein, dna binding protein |
| 由来する生物種 | Drosophila melanogaster (fruit fly) |
| 細胞内の位置 | Nucleus: P02836 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6619.54 |
| 構造登録者 | Clarke, N.D.,Kissinger, C.R.,Desjarlais, J.,Gilliland, G.L.,Pabo, C.O. (登録日: 1994-05-20, 公開日: 1994-08-31, 最終更新日: 2024-02-07) |
| 主引用文献 | Clarke, N.D.,Kissinger, C.R.,Desjarlais, J.,Gilliland, G.L.,Pabo, C.O. Structural studies of the engrailed homeodomain. Protein Sci., 3:1779-1787, 1994 Cited by PubMed Abstract: The structure of the Drosophila engrailed homeodomain has been solved by molecular replacement and refined to an R-factor of 19.7% at a resolution of 2.1 A. This structure offers a high-resolution view of an important family of DNA-binding proteins and allows comparison to the structure of the same protein bound to DNA. The most significant difference between the current structure and that of the 2.8-A engrailed-DNA complex is the close packing of an extended strand against the rest of the protein in the unbound protein. Structural features of the protein not previously noted include a "herringbone" packing of 4 aromatic residues in the core of the protein and an extensive network of salt bridges that covers much of the helix 1-helix 2 surface. Other features that may play a role in stabilizing the native state include the interaction of buried carbonyl oxygen atoms with the edge of Phe 49 and a bias toward statistically preferred side-chain dihedral angles. There is substantial disorder at both ends of the 61 amino acid protein. A 51-amino acid variant of engrailed (residues 6-56) was synthesized and shown by CD and thermal denaturation studies to be structurally and thermodynamically similar to the full-length domain. PubMed: 7849596主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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