1DCH
CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR
1DCH の概要
| エントリーDOI | 10.2210/pdb1dch/pdb |
| 分子名称 | DCOH (DIMERIZATION COFACTOR OF HNF-1), SULFATE ION (2 entities in total) |
| 機能のキーワード | transcriptional simulator, dimerization cofactor, dehydratase, 4a-carbinolamine dehydratase, transregulator of homeodomain proteins, transcriptional stimulator, dimerization |
| 由来する生物種 | Rattus norvegicus (Norway rat) |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 96909.33 |
| 構造登録者 | Endrizzi, J.A.,Cronk, J.D.,Wang, W.,Crabtree, G.R.,Alber, T. (登録日: 1995-01-24, 公開日: 1996-03-08, 最終更新日: 2024-02-07) |
| 主引用文献 | Endrizzi, J.A.,Cronk, J.D.,Wang, W.,Crabtree, G.R.,Alber, T. Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Science, 268:556-559, 1995 Cited by PubMed Abstract: DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates gene expression by associating with specific DNA binding proteins and also catalyzes the dehydration of the biopterin cofactor of phenylalanine hydroxylase. The x-ray crystal structure determined at 3 angstrom resolution reveals that DCoH forms a tetramer containing two saddle-shaped grooves that comprise likely macromolecule binding sites. Two equivalent enzyme active sites flank each saddle, suggesting that there is a spatial connection between the catalytic and binding activities. Structural similarities between the DCoH fold and nucleic acid-binding proteins argue that the saddle motif has evolved to bind diverse ligands or that DCoH unexpectedly may bind nucleic acids. PubMed: 7725101主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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