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Sea Anemone Peptide with Uncommon β-Hairpin Structure Inhibits Acid-sensing Ion Channel 3 (ASIC3) and Reveals Analgesic Activity
Three novel peptides were isolated from the venom of the sea anemone Urticina grebelnyi. All of them are 29 amino acid peptides cross-linked by two disulfide bridges, with a primary structure similar to other sea anemone peptides belonging to structural group 9a. The structure of the gene encoding t...
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| Autores principales: | , , , , , , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2013
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3743484/ https://ncbi.nlm.nih.gov/pubmed/23801332 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.485516 |
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