Molecular recognition of the neurotransmitter acetylcholine by an acetylcholine binding protein reveals determinants of binding to nicotinic acetylcholine receptors.
Despite extensive studies on nicotinic acetylcholine receptors (nAChRs) and homologues, details of acetylcholine binding are not completely resolved. Here, we report the crystal structure of acetylcholine bound to the receptor homologue acetylcholine binding protein from Lymnaea stagnalis. This is t...
I tiakina i:
| Ngā kaituhi matua: | , , , , |
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| Hōputu: | Artigo |
| Reo: | Inglês |
| I whakaputaina: |
Public Library of Science (PLoS)
2014-01-01
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| Rangatū: | PLoS ONE |
| Urunga tuihono: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24637639/?tool=EBI |
| Ngā Tūtohu: |
Kāore He Tūtohu, Me noho koe te mea tuatahi ki te tūtohu i tēnei pūkete!
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