1JS6
Crystal Structure of DOPA decarboxylase
Summary for 1JS6
| Entry DOI | 10.2210/pdb1js6/pdb |
| Related | 1JS3 |
| Descriptor | DOPA decarboxylase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | dopa decarboxylase, carbidopa, parkinson's disease, vitamin b6, lyase |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 2 |
| Total formula weight | 108498.63 |
| Authors | Burkhard, P.,Dominici, P.,Borri-Voltattorni, C.,Jansonius, J.N.,Malashkevich, V.N. (deposition date: 2001-08-16, release date: 2001-10-26, Last modification date: 2011-07-13) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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