6XYI

NMR solution structure of alpha-AnmTX- Ms11a-3 (Ms11a-3)

6XYI の概要

• エントリーDOI: 10.2210/pdb6xyi/pdb
• NMR情報: BMRB: 34486
• 分子名称: AMS9.3.1 (1 entity in total)
• 機能のキーワード: protein, toxin
• 由来する生物種: Metridium senile
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4936.89

構造登録者

Mineev, K.S.,Kornilov, F.D.,Lushpa, V.A.,Logashina, Y.A.,Maleeva, E.E.,Andreev, Y.A. (登録日: 2020-01-30, 公開日: 2021-02-10, 最終更新日: 2025-02-19)

主引用文献

Kasheverov, I.E.,Logashina, Y.A.,Kornilov, F.D.,Lushpa, V.A.,Maleeva, E.E.,Korolkova, Y.V.,Yu, J.,Zhu, X.,Zhangsun, D.,Luo, S.,Stensvag, K.,Kudryavtsev, D.S.,Mineev, K.S.,Andreev, Y.A.
Peptides from the Sea Anemone Metridium senile with Modified Inhibitor Cystine Knot (ICK) Fold Inhibit Nicotinic Acetylcholine Receptors.
Toxins, 15:-, 2022

PubMed Abstract: Nicotinic acetylcholine receptors (nAChRs) play an important role in the functioning of the central and peripheral nervous systems, and other organs of living creatures. There are several subtypes of nAChRs, and almost all of them are considered as pharmacological targets in different pathological states. The crude venom of the sea anemone showed the ability to interact with nAChRs. Four novel peptides (Ms11a-1-Ms11a-4) with nAChR binding activity were isolated. These peptides stabilized by three disulfide bridges have no noticeable homology with any known peptides. Ms11a-1-Ms11a-4 showed different binding activity towards the muscle-type nAChR from the ray. The study of functional activity and selectivity for the most potent peptide (Ms11a-3) revealed the highest antagonism towards the heterologous rat α9α10 nAChR compared to the muscle and α7 receptors. Structural NMR analysis of two toxins (Ms11a-2 and Ms11a-3) showed that they belong to a new variant of the inhibitor cystine knot (ICK) fold but have a prolonged loop between the fifth and sixth cysteine residues. Peptides Ms11a-1-Ms11a-4 could represent new pharmacological tools since they have structures different from other known nAChRs inhibitors.

PubMed: 36668848
DOI: 10.3390/toxins15010028

実験手法

SOLUTION NMR