Acetylcholine binding protein
From Proteopedia
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**[[2wnj]] - AcAChBP + DMXBA <br /> | **[[2wnj]] - AcAChBP + DMXBA <br /> | ||
**[[2wnl]] - AcAChBP + anabaseine <br /> | **[[2wnl]] - AcAChBP + anabaseine <br /> | ||
| - | **[[3u8j]], [[3u8k]], [[3u8l]], [[3u8n]] – LsAChBP + agonist<br /> | + | **[[3u8j]], [[3u8k]], [[3u8l]], [[3u8m]], [[3u8n]] – LsAChBP + agonist<br /> |
* AChBP+ions; Mimicking the ion conductance of the receptor | * AChBP+ions; Mimicking the ion conductance of the receptor | ||
| Line 72: | Line 72: | ||
* AChBP+ ligand homologs of the ligand acetylcholine | * AChBP+ ligand homologs of the ligand acetylcholine | ||
| + | **[[3wip]] - LsAChBP+ acetylcholine <br /> | ||
**[[1uv6]] - LsAChBP+ carbamylcholine <br /> | **[[1uv6]] - LsAChBP+ carbamylcholine <br /> | ||
**[[3zdg]], [[3zdh]] - LsAChBP+ carbamylcholine analog<br /> | **[[3zdg]], [[3zdh]] - LsAChBP+ carbamylcholine analog<br /> | ||
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**[[4bqt]] - AcAChBP+ cytisine<br /> | **[[4bqt]] - AcAChBP+ cytisine<br /> | ||
**[[2xz5]] – AcAChBP (mutant) + acetylcholine | **[[2xz5]] – AcAChBP (mutant) + acetylcholine | ||
| + | |||
| + | *AChBP+ modulator | ||
| + | |||
| + | **[[4nzb]] - LsAChBP+ NS9283 <br /> | ||
* AChBP+others | * AChBP+others | ||
**[[2br7]] - AcAChBP+ HEPES<br /> | **[[2br7]] - AcAChBP+ HEPES<br /> | ||
| - | **[[2y54]], [[2y56]], [[2y57]], [[2y58]] – AcAChBP residues 20-236 + azabicyclo-octan benzoate derivative | + | **[[2y54]], [[2y56]], [[2y57]], [[2y58]] – AcAChBP residues 20-236 + azabicyclo-octan benzoate derivative<br /> |
| + | **[[4qaa]], [[4qab]], [[4qac]] - LsAChBP+ aminopyrimidine derivative <br /> | ||
*AChBP α-7 | *AChBP α-7 | ||
| - | **[[3sq6]], [[3sq9]] – AchBP h/Ls chimera | + | **[[3sq6]], [[3sq9]] – AchBP h/Ls chimera<br /> |
| + | **[[4hqp]] - AchBP h/Ls chimera + bungrotoxin<br /> | ||
}} | }} | ||
Revision as of 12:11, 21 January 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 images on the left and 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 21-January-2015
Additional Resources
For additional information, see: Alzheimer's Disease
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, David Canner
