8JAF
Structure of Muscarinic receptor (M2R) in complex with beta-arrestin1 (Local Refine, non-cross linked)
Summary for 8JAF
| Entry DOI | 10.2210/pdb8jaf/pdb |
| EMDB information | 36126 |
| Descriptor | Beta-arrestin-1, Fab30 heavy chain, Fab30 light chain, ... (4 entities in total) |
| Functional Keywords | gpcr, arrestin, signaling protein, signaling protein-immune system complex, signaling protein/immune system |
| Biological source | Bos taurus (cattle) More |
| Total number of polymer chains | 4 |
| Total formula weight | 65592.97 |
| Authors | Maharana, J.,Sano, F.K.,Shihoya, W.,Banerjee, R.,Nureki, O.,Shukla, A.K. (deposition date: 2023-05-05, release date: 2023-12-27, Last modification date: 2024-10-23) |
| Primary citation | Maharana, J.,Sano, F.K.,Sarma, P.,Yadav, M.K.,Duan, L.,Stepniewski, T.M.,Chaturvedi, M.,Ranjan, A.,Singh, V.,Saha, S.,Mahajan, G.,Chami, M.,Shihoya, W.,Selent, J.,Chung, K.Y.,Banerjee, R.,Nureki, O.,Shukla, A.K. Molecular insights into atypical modes of beta-arrestin interaction with seven transmembrane receptors. Science, 383:101-108, 2024 Cited by PubMed Abstract: β-arrestins (βarrs) are multifunctional proteins involved in signaling and regulation of seven transmembrane receptors (7TMRs), and their interaction is driven primarily by agonist-induced receptor activation and phosphorylation. Here, we present seven cryo-electron microscopy structures of βarrs either in the basal state, activated by the muscarinic receptor subtype 2 (M2R) through its third intracellular loop, or activated by the βarr-biased decoy D6 receptor (D6R). Combined with biochemical, cellular, and biophysical experiments, these structural snapshots allow the visualization of atypical engagement of βarrs with 7TMRs and also reveal a structural transition in the carboxyl terminus of βarr2 from a β strand to an α helix upon activation by D6R. Our study provides previously unanticipated molecular insights into the structural and functional diversity encoded in 7TMR-βarr complexes with direct implications for exploring novel therapeutic avenues. PubMed: 38175886DOI: 10.1126/science.adj3347 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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