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TitleStructural insights into endogenous agonist selectivity of aminergic receptors from the octopamine beta 2 receptor.
Journal, issue, pagesPnas Nexus, Vol. 4, Year 2025
Publish dateMar 5, 2025 (structure data deposition date)
AuthorsTetsuya Hori / Kazushige Katsura / Sayako Miyamoto-Kohno / Tomomi Uchikubo-Kamo / Mayumi Yonemochi / Mikako Shirouzu /
PubMed AbstractTyrosine-derived amines (TDAs), such as octopamine, noradrenaline, dopamine, and tyramine, are essential neurotransmitters that play diverse roles in various physiological processes. The distinct ...Tyrosine-derived amines (TDAs), such as octopamine, noradrenaline, dopamine, and tyramine, are essential neurotransmitters that play diverse roles in various physiological processes. The distinct receptor selectivity of these structurally similar molecules is vital for their specific functions. However, all these receptors belong to the same subfamily of G-protein-coupled receptors and share high sequence homology within their orthosteric binding sites. The molecular basis of this selectivity remains unclear because of the absence of structural data on octopamine and tyramine receptors. In this study, we present cryo-electron microscopy structures of the deer tick octopamine β receptor (octβR) bound to octopamine or -2,4-dimethylphenyl-'-methylformamidine (DPMF), an acaricidal amitraz metabolite. Octopamine and DPMF formed aromatic interactions with Y307 and F328, residues crucial for octβR activation. The lower potency of other TDAs for octβR stems from the subtle effect of functional groups on both interactions, i.e. the meta-hydroxyl group of noradrenaline and dopamine hinders edge-to-edge interaction with Y307, and the absence of a 1-hydroxyl group in dopamine and tyramine prevents π-hydrogen bonding with F328. These structural insights into octβR selectivity are likely applicable across other TDA receptors, highlighting the pivotal role of residues 6.55 and 7.39. Consequently, the elucidated selection mechanism provides fundamental knowledge of aminergic ligand recognition, a process crucial for neurotransmission and overall organismal function.
External linksPnas Nexus / PubMed:41393170 / PubMed Central
MethodsEM (single particle)
Resolution3.39 - 3.65 Å
Structure data

PDB-9m55:
Structural insight into determinants of endogenous agonist selectivity of aminergic receptors from octopamine b2 receptor structure
Method: ELECTRON MICROSCOPY / Resolution: 3.39 Å

PDB-9m57:
Structural insight into determinants of endogenous agonist selectivity of aminergic receptors from octopamine b2 receptor structure
Method: ELECTRON MICROSCOPY / Resolution: 3.65 Å

Chemicals

PDB-1l8n:
The 1.5A crystal structure of alpha-D-glucuronidase from Bacillus stearothermophilus T-1, complexed with 4-O-methyl-glucuronic acid and xylotriose

ChemComp-OTR:
4-(2R-AMINO-1-HYDROXYETHYL)PHENOL

Source
  • ixodes scapularis (black-legged tick)
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / GPCR

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