7YMH
Cryo-EM structure of Nb29-alpha1AAR-miniGsq complex bound to noradrenaline
Summary for 7YMH
| Entry DOI | 10.2210/pdb7ymh/pdb |
| Related | 7YM8 |
| EMDB information | 33924 33928 |
| Descriptor | alpha1A-adrenergic receptor, miniGsq, Nb29, ... (4 entities in total) |
| Functional Keywords | gpcr, nanobody, agonist, complex, membrane protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 98293.98 |
| Authors | Toyoda, Y.,Zhu, A.,Yan, C.,Kobilka, B.K.,Liu, X. (deposition date: 2022-07-28, release date: 2023-07-05, Last modification date: 2024-10-09) |
| Primary citation | Toyoda, Y.,Zhu, A.,Kong, F.,Shan, S.,Zhao, J.,Wang, N.,Sun, X.,Zhang, L.,Yan, C.,Kobilka, B.K.,Liu, X. Structural basis of alpha 1A -adrenergic receptor activation and recognition by an extracellular nanobody. Nat Commun, 14:3655-3655, 2023 Cited by PubMed Abstract: The αadrenergic receptor (αAR) belongs to the family of G protein-coupled receptors that respond to adrenaline and noradrenaline. αAR is involved in smooth muscle contraction and cognitive function. Here, we present three cryo-electron microscopy structures of human αAR bound to the endogenous agonist noradrenaline, its selective agonist oxymetazoline, and the antagonist tamsulosin, with resolutions range from 2.9 Å to 3.5 Å. Our active and inactive αAR structures reveal the activation mechanism and distinct ligand binding modes for noradrenaline compared with other adrenergic receptor subtypes. In addition, we identified a nanobody that preferentially binds to the extracellular vestibule of αAR when bound to the selective agonist oxymetazoline. These results should facilitate the design of more selective therapeutic drugs targeting both orthosteric and allosteric sites in this receptor family. PubMed: 37339967DOI: 10.1038/s41467-023-39310-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.52 Å) |
Structure validation
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