8A5U
Crystal structure of the beta3 subunit extracellular domain of nicotinic acetylcholine receptor
Summary for 8A5U
| Entry DOI | 10.2210/pdb8a5u/pdb |
| Descriptor | Neuronal acetylcholine receptor subunit beta-3, 2-acetamido-2-deoxy-beta-D-glucopyranose, BICINE, ... (5 entities in total) |
| Functional Keywords | beta3 nicotinic acetylcholine receptor, pentameric receptors, ligand gated ion channels, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 26674.90 |
| Authors | Giastas, P.,Zouridakis, M. (deposition date: 2022-06-16, release date: 2022-08-10, Last modification date: 2024-11-13) |
| Primary citation | Giastas, P.,Papakyriakou, A.,Tsafaras, G.,Tzartos, S.J.,Zouridakis, M. Structural Insights into the Role of beta 3 nAChR Subunit in the Activation of Nicotinic Receptors. Molecules, 27:-, 2022 Cited by PubMed Abstract: The β3 subunit of nicotinic acetylcholine receptors (nAChRs) participates in heteropentameric assemblies with some α and other β neuronal subunits forming a plethora of various subtypes, differing in their electrophysiological and pharmacological properties. While β3 has for several years been considered an accessory subunit without direct participation in the formation of functional binding sites, recent electrophysiology data have disputed this notion and indicated the presence of a functional (+) side on the extracellular domain (ECD) of β3. In this study, we present the 2.4 Å resolution crystal structure of the monomeric β3 ECD, which revealed rather distinctive loop C features as compared to those of α nAChR subunits, leading to intramolecular stereochemical hindrance of the binding site cavity. Vigorous molecular dynamics simulations in the context of full length pentameric β3-containing nAChRs, while not excluding the possibility of a β3 (+) binding site, demonstrate that this site cannot efficiently accommodate the agonist nicotine. From the structural perspective, our results endorse the accessory rather than functional role of the β3 nAChR subunit, in accordance with earlier functional studies on β3-containing nAChRs. PubMed: 35889515DOI: 10.3390/molecules27144642 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
