8F04

Structure of elevenin-Vc1 from venom of the Australian cone snail Conus victoriae

8F04 の概要

• エントリーDOI: 10.2210/pdb8f04/pdb
• NMR情報: BMRB: 31054
• 分子名称: Elevenin-Vc1 (1 entity in total)
• 機能のキーワード: venom, hormone-like, hormone
• 由来する生物種: Conus victoriae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2125.61

構造登録者

Krishnarjuna, B.,Sunanda, P.,Norton, R.S. (登録日: 2022-11-01, 公開日: 2023-09-13, 最終更新日: 2024-11-06)

主引用文献

Krishnarjuna, B.,Sunanda, P.,Seow, J.,Tae, H.S.,Robinson, S.D.,Belgi, A.,Robinson, A.J.,Safavi-Hemami, H.,Adams, D.J.,Norton, R.S.
Characterisation of Elevenin-Vc1 from the Venom of Conus victoriae : A Structural Analogue of alpha-Conotoxins.
Mar Drugs, 21:-, 2023

PubMed Abstract: Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail ( , , 11-18). Although numerous elevenin sequences have been reported, their physiological function is unclear, and no structural information is available. Upon intracranial injection in mice, elevenin-Vc1 induced hyperactivity at doses of 5 or 10 nmol. The structure of elevenin-Vc1, determined using nuclear magnetic resonance spectroscopy, consists of a short helix and a bend region stabilised by the single disulfide bond. The elevenin-Vc1 structural fold is similar to that of α-conotoxins such as α-RgIA and α-ImI, which are also found in the venoms of cone snails and are antagonists at specific subtypes of nicotinic acetylcholine receptors (nAChRs). In an attempt to mimic the functional motif, Asp-Pro-Arg, of α-RgIA and α-ImI, we synthesised an analogue, designated elevenin-Vc1-DPR. However, neither elevenin-Vc1 nor the analogue was active at six different human nAChR subtypes (α1β1εδ, α3β2, α3β4, α4β2, α7, and α9α10) at 1 µM concentrations.

PubMed: 36827123
DOI: 10.3390/md21020081

実験手法

SOLUTION NMR