6OQP

U-AITx-Ate1

Summary for 6OQP

• Entry DOI: 10.2210/pdb6oqp/pdb
• NMR Information: BMRB: 30607
• Descriptor: SER-LYS-TRP-ILE-CYS-ALA-ASN-ARG-SER-VAL-CYS-PRO-ILE (1 entity in total)
• Functional Keywords: sea anemone cysteine-containing peptide structure nmr spectroscopy lipid interactions, antitumor protein
• Biological source: Actinia tenebrosa
• Total number of polymer chains: 1
• Total formula weight: 1478.78

Authors

Elnahriry, K.A.,Wai, D.C.C.,Norton, R.S. (deposition date: 2019-04-28, release date: 2019-07-31, Last modification date: 2024-11-06)

Primary citation

Elnahriry, K.A.,Wai, D.C.C.,Krishnarjuna, B.,Badawy, N.N.,Chittoor, B.,MacRaild, C.A.,Williams-Noonan, B.J.,Surm, J.M.,Chalmers, D.K.,Zhang, A.H.,Peigneur, S.,Mobli, M.,Tytgat, J.,Prentis, P.,Norton, R.S.
Structural and functional characterisation of a novel peptide from the Australian sea anemone Actinia tenebrosa.
Toxicon, 168:104-112, 2019

PubMed Abstract: Sea anemone venoms have long been recognised as a rich source of peptides with interesting pharmacological and structural properties. Our recent transcriptomic studies of the Australian sea anemone Actinia tenebrosa have identified a novel 13-residue peptide, U-AITx-Ate1. U-AITx-Ate1 contains a single disulfide bridge and bears no significant homology to previously reported amino acid sequences of peptides from sea anemones or other species. We have produced U-AITx-Ate1 using solid-phase peptide synthesis, followed by oxidative folding and purification of the folded peptide using reversed-phase high-performance liquid chromatography. The solution structure of U-AITx-Ate1 was determined based on two-dimensional nuclear magnetic resonance spectroscopic data. Diffusion-ordered NMR spectroscopy revealed that U-AITx-Ate1 was monomeric in solution. Perturbations in the 1D H NMR spectrum of U-AITx-Ate1 in the presence of dodecylphosphocholine micelles together with molecular dynamics simulations indicated an interaction of U-AITx-Ate1 with lipid membranes, although no binding was detected to 100% POPC and 80% POPC: 20% POPG lipid nanodiscs by isothermal titration calorimetry. Functional assays were performed to explore the biological activity profile of U-AITx-Ate1. U-AITx-Ate1 showed no activity in voltage-clamp electrophysiology assays and no change in behaviour and mortality rates in crustacea. Moderate cytotoxic activity was observed against two breast cancer cell lines.

PubMed: 31302115
DOI: 10.1016/j.toxicon.2019.07.002

Experimental method

SOLUTION NMR