Acetylcholine binding protein
From Proteopedia
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{{STRUCTURE_2byn| PDB=2byn | SIZE=400| SCENE=Acetylcholine_binding_protein/Cv/1 |right|CAPTION=Acetylcholine binding protein pentamer complex with PEG [[2byn]] }} | {{STRUCTURE_2byn| PDB=2byn | SIZE=400| SCENE=Acetylcholine_binding_protein/Cv/1 |right|CAPTION=Acetylcholine binding protein pentamer complex with PEG [[2byn]] }} | ||
| - | [[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). The crystal structure of the 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 | + | [[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). The crystal structure of the 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 image on the right correspond to one representative AChBP structure, ''i.e.'' the Acetylcholine binding protein from ''Aplysia californica'' ([[2byn]]). |
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Revision as of 11:38, 17 May 2015
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). The crystal structure of the 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 image on the right correspond to one representative AChBP structure, i.e. the Acetylcholine binding protein from Aplysia californica (2byn).
3D Structures of Acetylcholine binding protein
Updated on 17-May-2015
Additional Resources
For additional information, see: Alzheimer's Disease
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Michal Harel, Alexander Berchansky, Joel L. Sussman, David Canner
