6BL9

NMR Solution structure of U-SLPTX15-Sm2a

6BL9 の概要

• エントリーDOI: 10.2210/pdb6bl9/pdb
• NMR情報: BMRB: 30372
• 分子名称: Sm2a toxin (1 entity in total)
• 機能のキーワード: scorpion toxin csab fold, toxin
• 由来する生物種: Scolopendra morsitans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6007.70

構造登録者

Harvey, P.J.,Craik, D.J.,Durek, T.,Dash, T.J. (登録日: 2017-11-09, 公開日: 2018-11-14, 最終更新日: 2024-11-06)

主引用文献

Dash, T.S.,Shafee, T.,Harvey, P.J.,Zhang, C.,Peigneur, S.,Deuis, J.R.,Vetter, I.,Tytgat, J.,Anderson, M.A.,Craik, D.J.,Durek, T.,Undheim, E.A.B.
A Centipede Toxin Family Defines an Ancient Class of CS alpha beta Defensins.
Structure, 27:315-326.e7, 2019

PubMed Abstract: Disulfide-rich peptides (DRPs) play diverse physiological roles and have emerged as attractive sources of pharmacological tools and drug leads. Here we describe the 3D structure of a centipede venom peptide, U-SLPTX-Sm2a, whose family defines a unique class of one of the most widespread DRP folds known, the cystine-stabilized α/β fold (CSαβ). This class, which we have named the two-disulfide CSαβ fold (2ds-CSαβ), contains only two internal disulfide bonds as opposed to at least three in all other confirmed CSαβ peptides, and constitutes one of the major neurotoxic peptide families in centipede venoms. We show the 2ds-CSαβ is widely distributed outside centipedes and is likely an ancient fold predating the split between prokaryotes and eukaryotes. Our results provide insights into the ancient evolutionary history of a widespread DRP fold and highlight the usefulness of 3D structures as evolutionary tools.

PubMed: 30554841
DOI: 10.1016/j.str.2018.10.022

実験手法

SOLUTION NMR