Acetylcholine binding protein

spinqualitylabelsall models Lymnaea acetylcholine-binding protein pentamer complex with acetylcholine (PDB code 3wip) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Acetylcholine binding protein (AChBP) is secreted by snails into cholinergic synapses, where it modulates transmission by binding acetylcholine (ACh). Sequence alignment revealed high similarity to the extracellular domains of the ligand-binding subunits of the nicotinic acetylcholine receptor (nAChR). AChBP alpha7 is highly similar to the ligand-binding domain of nAChR alpha7. See also - Acetylcholine Receptor and its Reaction to Cobra Venom Binding site of AChR. Structural highlights The crystal structures of the Lymnaea stagnalis and the Aplysia californica AChBP homopentamer indeed provides a valuable model for identifying the nature of the ligand-binding domains and of the subunit interfaces of the nAChR. Furthermore, crystal structures of complexes of AChBP with various agonists and antagonists have provided detailed insight into the neurotransmitter binding site of nAChRs. The binding site of AChBP is located at the interface of neighboring subunits. Chain A is in cyan, chain B is in salmon, ACh is in yellow. Relevance Like the nAChR, AChBP - with ca. 20% sequence similarity - binds agonists and antagonists like ACh , nicotine , α-bungarotoxin , epibatidine with similar affinities hence it is a useful tool for understanding nAChR activity. Both receptors contain a Cys-Cys loop at the subunits interface as well as conserved residues at the ACh binding site. 3D Structures of Acetylcholine binding protein Acetylcholine binding protein 3D structures

Additional Resources

For additional information, see: Acetylcholine Receptor and its Reaction to Cobra Venom

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Joel L. Sussman, Alexander Berchansky, David Canner, Michal Harel