9ASA
Global reconstruction of 5-HT2AR bound to RS130-180 in complex with a mini-Gq protein and scFv16 obtained by cryo-electron microscopy (cryoEM)
This is a non-PDB format compatible entry.
Summary for 9ASA
| Entry DOI | 10.2210/pdb9asa/pdb |
| EMDB information | 43810 |
| Descriptor | 5-hydroxytryptamine receptor 2A, G subunit q (Gi2-mini-Gq chimeric), Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (6 entities in total) |
| Functional Keywords | gpcr, g-protein coupled receptor, 5-ht2ar, serotonin, psychedelics, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 157050.40 |
| Authors | Gumpper, R.H.,Fay, J.F.,Roth, B.L. (deposition date: 2024-02-24, release date: 2025-04-02, Last modification date: 2025-05-21) |
| Primary citation | Gumpper, R.H.,Jain, M.K.,Kim, K.,Sun, R.,Sun, N.,Xu, Z.,DiBerto, J.F.,Krumm, B.E.,Kapolka, N.J.,Kaniskan, H.U.,Nichols, D.E.,Jin, J.,Fay, J.F.,Roth, B.L. The structural diversity of psychedelic drug actions revealed. Nat Commun, 16:2734-2734, 2025 Cited by PubMed Abstract: There is currently a resurgence in exploring the utility of classical psychedelics to treat depression, addiction, anxiety disorders, cluster headaches, and many other neuropsychiatric disorders. A biological target of these compounds, and a hypothesized target for their therapeutic actions, is the 5-HT serotonin receptor. Here, we present 7 cryo-EM structures covering all major compound classes of psychedelic and non-psychedelic agonists, including a β-arrestin-biased compound RS130-180. Identifying the molecular interactions between various psychedelics and the 5-HT receptor reveals both common and distinct motifs among the examined psychedelic chemotypes. These findings lead to a broader mechanistic understanding of 5-HT activation, which can catalyze the development of novel chemotypes with potential therapeutic utility and fewer side effects. PubMed: 40108183DOI: 10.1038/s41467-025-57956-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.12 Å) |
Structure validation
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