2MUN

Solution structure of mu-SLPTX3-Ssm6a

2MUN の概要

• エントリーDOI: 10.2210/pdb2mun/pdb
• NMR情報: BMRB: 25223
• 分子名称: Mu-scoloptoxin-Ssm6a (1 entity in total)
• 機能のキーワード: toxin, mu-slptx-ssm6a, crustacean hyperglycemic hormone, ion channel inhibitor
• 由来する生物種: Scolopendra mutilans (Chinese red-headed centipede)
• 細胞内の位置: Secreted: P0DL36
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5333.00

構造登録者

Undheim, E.A.B.,King, G.F.,Mobli, M. (登録日: 2014-09-13, 公開日: 2015-06-24, 最終更新日: 2024-11-20)

主引用文献

Undheim, E.A.,Grimm, L.L.,Low, C.F.,Morgenstern, D.,Herzig, V.,Zobel-Thropp, P.,Pineda, S.S.,Habib, R.,Dziemborowicz, S.,Fry, B.G.,Nicholson, G.M.,Binford, G.J.,Mobli, M.,King, G.F.
Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators.
Structure, 23:1283-1292, 2015

PubMed Abstract: Arthropod venoms consist primarily of peptide toxins that are injected into their prey with devastating consequences. Venom proteins are thought to be recruited from endogenous body proteins and mutated to yield neofunctionalized toxins with remarkable affinity for specific subtypes of ion channels and receptors. However, the evolutionary history of venom peptides remains poorly understood. Here we show that a neuropeptide hormone has been convergently recruited into the venom of spiders and centipedes and evolved into a highly stable toxin through divergent modification of the ancestral gene. High-resolution structures of representative hormone-derived toxins revealed they possess a unique structure and disulfide framework and that the key structural adaptation in weaponization of the ancestral hormone was loss of a C-terminal α helix, an adaptation that occurred independently in spiders and centipedes. Our results raise a new paradigm for toxin evolution and highlight the value of structural information in providing insight into protein evolution.

PubMed: 26073605
DOI: 10.1016/j.str.2015.05.003

実験手法

SOLUTION NMR