4XPT
X-ray structure of Drosophila dopamine transporter with subsiteB mutations D121G/S426M and EL2 deletion of 162-201 in complex with substrate analogue 3,4 dichlorophen ethylamine
Summary for 4XPT
| Entry DOI | 10.2210/pdb4xpt/pdb |
| Related | 4M48 4XNU 4XNX 4XP1 4XP4 4XP5 4XP6 4XP9 4XPA 4XPB 4XPF 4XPG 4XPH |
| Related PRD ID | PRD_900018 |
| Descriptor | Dopamine transporter, SODIUM ION, antibody fragment light chain, ... (10 entities in total) |
| Functional Keywords | integral membrane protein, all-alpha helical antidepressant complex, transport protein-inhibitor complex, protein transport-inhibitor complex, protein transport/inhibitor |
| Biological source | Drosophila melanogaster (Fruit fly) More |
| Total number of polymer chains | 3 |
| Total formula weight | 109981.09 |
| Authors | Aravind, P.,Wang, K.,Gouaux, E. (deposition date: 2015-01-17, release date: 2015-05-06, Last modification date: 2024-10-09) |
| Primary citation | Wang, K.H.,Penmatsa, A.,Gouaux, E. Neurotransmitter and psychostimulant recognition by the dopamine transporter. Nature, 521:322-327, 2015 Cited by PubMed Abstract: Na(+)/Cl(-)-coupled biogenic amine transporters are the primary targets of therapeutic and abused drugs, ranging from antidepressants to the psychostimulants cocaine and amphetamines, and to their cognate substrates. Here we determine X-ray crystal structures of the Drosophila melanogaster dopamine transporter (dDAT) bound to its substrate dopamine, a substrate analogue 3,4-dichlorophenethylamine, the psychostimulants d-amphetamine and methamphetamine, or to cocaine and cocaine analogues. All ligands bind to the central binding site, located approximately halfway across the membrane bilayer, in close proximity to bound sodium and chloride ions. The central binding site recognizes three chemically distinct classes of ligands via conformational changes that accommodate varying sizes and shapes, thus illustrating molecular principles that distinguish substrates from inhibitors in biogenic amine transporters. PubMed: 25970245DOI: 10.1038/nature14431 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.36 Å) |
Structure validation
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