8hti | pdb_00008hti
Human Consensus Olfactory Receptor OR52c in Complex with Octanoic Acid (OCA) and G Protein
Structural highlights
FunctionGBB1_HUMAN Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.[1] Publication Abstract from PubMedStructural and mechanistic studies on human odorant receptors (ORs), key in olfactory signaling, are challenging because of their low surface expression in heterologous cells. The recent structure of OR51E2 bound to propionate provided molecular insight into odorant recognition, but the lack of an inactive OR structure limited understanding of the activation mechanism of ORs upon odorant binding. Here, we determined the cryo-electron microscopy structures of consensus OR52 (OR52(cs)), a representative of the OR52 family, in the ligand-free (apo) and octanoate-bound states. The apo structure of OR52(cs) reveals a large opening between transmembrane helices (TMs) 5 and 6. A comparison between the apo and active structures of OR52(cs) demonstrates the inward and outward movements of the extracellular and intracellular segments of TM6, respectively. These results, combined with molecular dynamics simulations and signaling assays, shed light on the molecular mechanisms of odorant binding and activation of the OR52 family. Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family.,Choi C, Bae J, Kim S, Lee S, Kang H, Kim J, Bang I, Kim K, Huh WK, Seok C, Park H, Im W, Choi HJ Nat Commun. 2023 Dec 7;14(1):8105. doi: 10.1038/s41467-023-43983-9. PMID:38062020[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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