5LAH

NMR structure of the sea anemone peptide tau-AnmTx Ueq 12-1 with an uncommon fold

Summary for 5LAH

• Entry DOI: 10.2210/pdb5lah/pdb
• NMR Information: BMRB: 34008
• Descriptor: tau-AnmTx Ueq 12-1 (1 entity in total)
• Functional Keywords: protein, sea anemone, antimicrobial peptide, trpa1 potentiator, membrane protein, toxin
• Biological source: Urticina eques
• Total number of polymer chains: 1
• Total formula weight: 4808.26

Authors

Mineev, K.S.,Arseniev, A.S.,Andreev, Y.A.,Kozlov, S.A.,Logashina, Y.A. (deposition date: 2016-06-14, release date: 2017-05-10, Last modification date: 2024-11-13)

Primary citation

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.
New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties
Toxins, 9:154-, 2017

PubMed Abstract: A novel bioactive peptide named τ-AnmTx Ueq 12-1 (short name Ueq 12-1) was isolated and characterized from the sea anemone Ueq 12-1 is unique among the variety of known sea anemone peptides in terms of its primary and spatial structure. It consists of 45 amino acids including 10 cysteine residues with an unusual distribution and represents a new group of sea anemone peptides. The 3D structure of Ueq 12-1, determined by NMR spectroscopy, represents a new disulfide-stabilized fold partly similar to the defensin-like fold. Ueq 12-1 showed the dual activity of both a moderate antibacterial activity against Gram-positive bacteria and a potentiating activity on the transient receptor potential ankyrin 1 (TRPA1). Ueq 12-1 is a unique peptide potentiator of the TRPA1 receptor that produces analgesic and anti-inflammatory effects . The antinociceptive properties allow us to consider Ueq 12-1 as a potential analgesic drug lead with antibacterial properties.

PubMed: 28468269
DOI: 10.3390/toxins9050154

Experimental method

SOLUTION NMR