8POK
Cryo-EM structure of cell-free synthesized human histamine H2 receptor coupled to heterotrimeric Gs protein in lipid environment
Summary for 8POK
| Entry DOI | 10.2210/pdb8pok/pdb |
| EMDB information | 17793 |
| Descriptor | Histamine H2 receptor, Isoform Gnas-2 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (6 entities in total) |
| Functional Keywords | gpcr, cell-free, h2r, human histamine 2 receptor, active conformation, complex, detergent-free, lipid environment, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 146866.99 |
| Authors | Schnelle, K.,Koeck, Z.,Persechino, M.,Umbach, S.,Schihada, H.,Januliene, D.,Parey, K.,Pockes, S.,Kolb, P.,Doetsch, V.,Moeller, A.,Hilger, D.,Bernhard, F. (deposition date: 2023-07-05, release date: 2024-03-06, Last modification date: 2025-07-02) |
| Primary citation | Kock, Z.,Schnelle, K.,Persechino, M.,Umbach, S.,Schihada, H.,Januliene, D.,Parey, K.,Pockes, S.,Kolb, P.,Dotsch, V.,Moller, A.,Hilger, D.,Bernhard, F. Cryo-EM structure of cell-free synthesized human histamine 2 receptor/G s complex in nanodisc environment. Nat Commun, 15:1831-1831, 2024 Cited by PubMed Abstract: Here we describe the cryo-electron microscopy structure of the human histamine 2 receptor (HR) in an active conformation with bound histamine and in complex with G heterotrimeric protein at an overall resolution of 3.4 Å. The complex was generated by cotranslational insertion of the receptor into preformed nanodisc membranes using cell-free synthesis in E. coli lysates. Structural comparison with the inactive conformation of HR and the inactive and G-coupled active state of HR together with structure-guided functional experiments reveal molecular insights into the specificity of ligand binding and G protein coupling for this receptor family. We demonstrate lipid-modulated folding of cell-free synthesized HR, its agonist-dependent internalization and its interaction with endogenously synthesized HR and HR in HEK293 cells by applying a recently developed nanotransfer technique. PubMed: 38418462DOI: 10.1038/s41467-024-46096-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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