6G79
Coupling specificity of heterotrimeric Go to the serotonin 5-HT1B receptor
Summary for 6G79
| Entry DOI | 10.2210/pdb6g79/pdb |
| EMDB information | 4358 |
| Descriptor | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Guanine nucleotide-binding protein G(o) subunit alpha, ... (5 entities in total) |
| Functional Keywords | g-protein coupled receptor, 5-ht1b, mini-go, serotonin, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 111964.40 |
| Authors | Garcia-Nafria, J.,Nehme, R.,Edwards, P.,Tate, C.G. (deposition date: 2018-04-05, release date: 2018-06-20, Last modification date: 2024-11-13) |
| Primary citation | Garcia-Nafria, J.,Nehme, R.,Edwards, P.C.,Tate, C.G. Cryo-EM structure of the serotonin 5-HT1Breceptor coupled to heterotrimeric Go. Nature, 558:620-623, 2018 Cited by PubMed Abstract: G-protein-coupled receptors (GPCRs) form the largest family of receptors encoded by the human genome (around 800 genes). They transduce signals by coupling to a small number of heterotrimeric G proteins (16 genes encoding different α-subunits). Each human cell contains several GPCRs and G proteins. The structural determinants of coupling of G to four different GPCRs have been elucidated, but the molecular details of how the other G-protein classes couple to GPCRs are unknown. Here we present the cryo-electron microscopy structure of the serotonin 5-HT receptor (5-HTR) bound to the agonist donitriptan and coupled to an engineered G heterotrimer. In this complex, 5-HTR is in an active state; the intracellular domain of the receptor is in a similar conformation to that observed for the β-adrenoceptor (βAR) or the adenosine A receptor (AR) in complex with G. In contrast to the complexes with G, the gap between the receptor and the Gβ-subunit in the G-5-HTR complex precludes molecular contacts, and the interface between the Gα-subunit of G and the receptor is considerably smaller. These differences are likely to be caused by the differences in the interactions with the C terminus of the G α-subunit. The molecular variations between the interfaces of G and G in complex with GPCRs may contribute substantially to both the specificity of coupling and the kinetics of signalling. PubMed: 29925951DOI: 10.1038/s41586-018-0241-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.78 Å) |
Structure validation
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