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TitleStructural and functional basis of antinociceptive action of χ-conotoxin AoIA at the noradrenaline transporter.
Journal, issue, pagesNat Struct Mol Biol, Year 2026
Publish dateJul 21, 2026
AuthorsOliver J V Belleza / Heng Zhang / Helmut Schmidhammer / Tye I Gonzalez / Cosmin I Ciotu / Nataša Tomašević / Carlo Martin M Ocampo / Jomari C Fernando / Johannes Koehbach / Paula Schwarz / Mounaf Al Makhlouf / Gabor Tajti / Simon Hasinger / Nina Kastner / Orcun Avsar / Bernhard Retzl / Kathrin Jäntsch / Yi Jiang / Roland Hellinger / Michael J M Fischer / K Johan Rosengren / Christian W Gruber / Aaron Joseph L Villaraza / Thomas Stockner / Mariana Spetea / H Eric Xu / Harald H Sitte /
PubMed AbstractThe χ-conotoxins are venom-derived peptides that specifically target the noradrenaline transporter (also known as norepinephrine transporter, NET). Regulation of noradrenergic signaling by NET ...The χ-conotoxins are venom-derived peptides that specifically target the noradrenaline transporter (also known as norepinephrine transporter, NET). Regulation of noradrenergic signaling by NET affects neurophysiological processes, including pain. Therefore, the χ-conotoxin MrIA and its synthetic analogs have been previously investigated for their analgesic activity. Here we describe the synthesis and pharmacological characterization of χ-AoIA, a peptide that selectively inhibits NET with a higher potency compared to MrIA in in vitro radiotracer flux assays. Furthermore, we resolved the structure of the human NET:χ-AoIA complex by cryogenic electron microscopy, which revealed an atypical binding mode consisting of both the central binding site and the outer vestibule of the transporter. Lastly, χ-AoIA displays antinociceptive efficacy in a model of inflammatory pain after subcutaneous administration in mice. Our results demonstrate the efficacy of χ-AoIA as a highly selective ligand of NET and provide a mechanistic basis for its potential development as a nonopioid analgesic.
External linksNat Struct Mol Biol / PubMed:42481720
MethodsEM (single particle) / NMR (solution)
Resolution2.77 Å
Structure data

62139

9k6x

EMDB-62139, PDB-9k6x:
Structural and functional basis of antinociceptive action of conotoxin AoIA at the noradrenaline transporter
Method: EM (single particle) / Resolution: 2.77 Å

PDB-9paz:
Solution NMR structure of conotoxin AoIA
Method: SOLUTION NMR

PDB-9pb0:
Solution NMR structure of conotoxin AoIA - globular disulfide isomer
Method: SOLUTION NMR

Chemicals

PDB-1eet:
HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH THE INHIBITOR MSC204

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
  • conus marmoreus (invertebrata)
  • conus araneosus (invertebrata)
KeywordsTRANSPORT PROTEIN / Complex / TOXIN / conotoxin / chi-conotoxin / NET-inhibitor

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