6OIJ
Muscarinic acetylcholine receptor 1-G11 protein complex
Summary for 6OIJ
Entry DOI | 10.2210/pdb6oij/pdb |
EMDB information | 20078 |
Descriptor | Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein subunit alpha-11, Muscarinic acetylcholine receptor M1, Antibody fragment, ... (7 entities in total) |
Functional Keywords | g-protein coupled receptor-g-protein complex, neurotransmitter receptor, signaling protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 5 |
Total formula weight | 156612.83 |
Authors | Maeda, S.,Qianhui, Q.,Skiniotis, G.,Kobilka, B. (deposition date: 2019-04-09, release date: 2019-05-08, Last modification date: 2020-01-08) |
Primary citation | Maeda, S.,Qu, Q.,Robertson, M.J.,Skiniotis, G.,Kobilka, B.K. Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes. Science, 364:552-557, 2019 Cited by PubMed Abstract: Muscarinic acetylcholine receptors are G protein-coupled receptors that respond to acetylcholine and play important signaling roles in the nervous system. There are five muscarinic receptor subtypes (M1R to M5R), which, despite sharing a high degree of sequence identity in the transmembrane region, couple to different heterotrimeric GTP-binding proteins (G proteins) to transmit signals. M1R, M3R, and M5R couple to the G family, whereas M2R and M4R couple to the G family. Here, we present and compare the cryo-electron microscopy structures of M1R in complex with G and M2R in complex with G The M1R-G complex exhibits distinct features, including an extended transmembrane helix 5 and carboxyl-terminal receptor tail that interacts with G protein. Detailed analysis of these structures provides a framework for understanding the molecular determinants of G-protein coupling selectivity. PubMed: 31073061DOI: 10.1126/science.aaw5188 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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