8F04
Structure of elevenin-Vc1 from venom of the Australian cone snail Conus victoriae
Summary for 8F04
| Entry DOI | 10.2210/pdb8f04/pdb |
| NMR Information | BMRB: 31054 |
| Descriptor | Elevenin-Vc1 (1 entity in total) |
| Functional Keywords | venom, hormone-like, hormone |
| Biological source | Conus victoriae |
| Total number of polymer chains | 1 |
| Total formula weight | 2125.61 |
| Authors | Krishnarjuna, B.,Sunanda, P.,Norton, R.S. (deposition date: 2022-11-01, release date: 2023-09-13, Last modification date: 2024-11-06) |
| Primary citation | 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 Cited by 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: 36827123DOI: 10.3390/md21020081 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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