6OVJ

NMR structure of truncated alpha conotoxin SII: Ile-SII(3-14)

6OVJ の概要

• エントリーDOI: 10.2210/pdb6ovj/pdb
• 関連するPDBエントリー: 6OTB
• 分子名称: Alpha-conotoxin S2 (1 entity in total)
• 機能のキーワード: toxin
• 由来する生物種: Conus striatus (Striated cone)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1314.54

構造登録者

Chin, Y.K.-Y.,Wilhelm, P.,Alewood, P.F. (登録日: 2019-05-08, 公開日: 2020-05-06, 最終更新日: 2024-11-20)

主引用文献

Wilhelm, P.,Luna-Ramirez, K.,Chin, Y.K.,Dekan, Z.,Abraham, N.,Tae, H.S.,Chow, C.Y.,Eagles, D.A.,King, G.F.,Lewis, R.J.,Adams, D.J.,Alewood, P.F.
Cysteine-Rich alpha-Conotoxin SII Displays Novel Interactions at the Muscle Nicotinic Acetylcholine Receptor.
Acs Chem Neurosci, 13:1245-1250, 2022

PubMed Abstract: α-Conotoxins that target muscle nicotinic acetylcholine receptors (nAChRs) commonly fall into two structural classes, frameworks I and II containing two and three disulfide bonds, respectively. Conotoxin SII is the sole member of the cysteine-rich framework II with ill-defined interactions at the nAChRs. Following directed synthesis of α-SII, NMR analysis revealed a well-defined structure containing a 3-helix frequently employed by framework I α-conotoxins; α-SII acted at the muscle nAChR with half-maximal inhibitory concentrations (IC) of 120 nM (adult) and 370 nM (fetal) though weakly at neuronal nAChRs. Truncation of α-SII to a two disulfide bond amidated peptide with framework I disulfide connectivity led to similar activity. Surprisingly, the more constrained α-SII was less stable under mild reducing conditions and displayed a unique docking mode at the nAChR.

PubMed: 35357806
DOI: 10.1021/acschemneuro.1c00857

実験手法

SOLUTION NMR