1JS6
Crystal Structure of DOPA decarboxylase
1JS6 の概要
| エントリーDOI | 10.2210/pdb1js6/pdb |
| 関連するPDBエントリー | 1JS3 |
| 分子名称 | DOPA decarboxylase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| 機能のキーワード | dopa decarboxylase, carbidopa, parkinson's disease, vitamin b6, lyase |
| 由来する生物種 | Sus scrofa (pig) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 108498.63 |
| 構造登録者 | Burkhard, P.,Dominici, P.,Borri-Voltattorni, C.,Jansonius, J.N.,Malashkevich, V.N. (登録日: 2001-08-16, 公開日: 2001-10-26, 最終更新日: 2025-03-26) |
| 主引用文献 | Burkhard, P.,Dominici, P.,Borri-Voltattorni, C.,Jansonius, J.N.,Malashkevich, V.N. Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Nat.Struct.Biol., 8:963-967, 2001 Cited by PubMed Abstract: DOPA decarboxylase (DDC) is responsible for the synthesis of the key neurotransmitters dopamine and serotonin via decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan, respectively. DDC has been implicated in a number of clinic disorders, including Parkinson's disease and hypertension. Peripheral inhibitors of DDC are currently used to treat these diseases. We present the crystal structures of ligand-free DDC and its complex with the anti-Parkinson drug carbiDOPA. The inhibitor is bound to the enzyme by forming a hydrazone linkage with the cofactor, and its catechol ring is deeply buried in the active site cleft. The structures provide the molecular basis for the development of new inhibitors of DDC with better pharmacological characteristics. PubMed: 11685243DOI: 10.1038/nsb1101-963 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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