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TitleNew Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties
Journal, issue, pagesToxins, Vol. 9, Page 154-, Year 2017
Publish dateJun 14, 2016 (structure data deposition date)
AuthorsLogashina, Y.A. / Solstad, R.G. / Mineev, K.S. / Korolkova, Y.V. / Mosharova, I.V. / Dyachenko, I.A. / Palikov, V.A. / Palikova, Y.A. / Murashev, A.N. / Arseniev, A.S. ...Logashina, Y.A. / Solstad, R.G. / Mineev, K.S. / Korolkova, Y.V. / Mosharova, I.V. / Dyachenko, I.A. / Palikov, V.A. / Palikova, Y.A. / Murashev, A.N. / Arseniev, A.S. / Kozlov, S.A. / Stensvag, K. / Haug, T. / Andreev, Y.A.
External linksToxins / PubMed:28468269
MethodsNMR (solution)
Structure data

PDB-5lah:
NMR structure of the sea anemone peptide tau-AnmTx Ueq 12-1 with an uncommon fold
Method: SOLUTION NMR

Source
  • urticina eques (sea anemone)
KeywordsTOXIN / PROTEIN / sea anemone / antimicrobial peptide / TRPA1 potentiator / membrane protein

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