2MIX
Structure of a novel venom peptide toxin from sample limited terebrid marine snail
Summary for 2MIX
| Entry DOI | 10.2210/pdb2mix/pdb |
| NMR Information | BMRB: 19697 |
| Descriptor | venom peptide toxin (1 entity in total) |
| Functional Keywords | teretoxin, peptide toxin, toxin |
| Biological source | Terebridae (sea snail) |
| Total number of polymer chains | 1 |
| Total formula weight | 2318.68 |
| Authors | Bhuiyan, M.H.,Anand, P.,Grigoryan, A.,Holford, M.,Poget, S.F. (deposition date: 2013-12-20, release date: 2014-12-03, Last modification date: 2023-06-14) |
| Primary citation | Anand, P.,Grigoryan, A.,Bhuiyan, M.H.,Ueberheide, B.,Russell, V.,Quinonez, J.,Moy, P.,Chait, B.T.,Poget, S.F.,Holford, M. Sample limited characterization of a novel disulfide-rich venom peptide toxin from terebrid marine snail Terebra variegata. Plos One, 9:e94122-e94122, 2014 Cited by PubMed Abstract: Disulfide-rich peptide toxins found in the secretions of venomous organisms such as snakes, spiders, scorpions, leeches, and marine snails are highly efficient and effective tools for novel therapeutic drug development. Venom peptide toxins have been used extensively to characterize ion channels in the nervous system and platelet aggregation in haemostatic systems. A significant hurdle in characterizing disulfide-rich peptide toxins from venomous animals is obtaining significant quantities needed for sequence and structural analyses. Presented here is a strategy for the structural characterization of venom peptide toxins from sample limited (4 ng) specimens via direct mass spectrometry sequencing, chemical synthesis and NMR structure elucidation. Using this integrated approach, venom peptide Tv1 from Terebra variegata was discovered. Tv1 displays a unique fold not witnessed in prior snail neuropeptides. The novel structural features found for Tv1 suggest that the terebrid pool of peptide toxins may target different neuronal agents with varying specificities compared to previously characterized snail neuropeptides. PubMed: 24713808DOI: 10.1371/journal.pone.0094122 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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