Summary for 8XTY
| Entry DOI | 10.2210/pdb8xty/pdb |
| EMDB information | 38653 |
| Descriptor | Vesicular acetylcholine transporter,Green fluorescent protein,antibody, vesamicol (2 entities in total) |
| Functional Keywords | transporter, membrane protein, transport protein, transport protein-inhibitor complex, transport protein/inhibitor |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 92203.81 |
| Authors | |
| Primary citation | Ma, Q.,Ma, K.,Dong, Y.,Meng, Y.,Zhao, J.,Li, R.,Bai, Q.,Wu, D.,Jiang, D.,Sun, J.,Zhao, Y. Binding mechanism and antagonism of the vesicular acetylcholine transporter VAChT. Nat.Struct.Mol.Biol., 32:818-827, 2025 Cited by PubMed Abstract: The vesicular acetylcholine transporter (VAChT) has a pivotal role in packaging and transporting acetylcholine for exocytotic release, serving as a vital component of cholinergic neurotransmission. Dysregulation of its function can result in neurological disorders. It also serves as a target for developing radiotracers to quantify cholinergic neuron deficits in neurodegenerative conditions. Here we unveil the cryo-electron microscopy structures of human VAChT in its apo state, the substrate acetylcholine-bound state and the inhibitor vesamicol-bound state. These structures assume a lumen-facing conformation, offering a clear depiction of architecture of VAChT. The acetylcholine-bound structure provides a detailed understanding of how VAChT recognizes its substrate, shedding light on the coupling mechanism of protonation and substrate binding. Meanwhile, the vesamicol-bound structure reveals the binding mode of vesamicol to VAChT, laying the structural foundation for the design of the next generation of radioligands targeting VAChT. PubMed: 39806024DOI: 10.1038/s41594-024-01462-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
Download full validation report
