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2MSF

NMR SOLUTION STRUCTURE OF SCORPION VENOM TOXIN Ts11 (TsPep1) FROM Tityus serrulatus

2MSF の概要
エントリーDOI10.2210/pdb2msf/pdb
NMR情報BMRB: 25122
分子名称Peptide TsPep1 (1 entity in total)
機能のキーワードtoxin
由来する生物種Tityus serrulatus (Brazilian scorpion)
細胞内の位置Secreted: P0C174
タンパク質・核酸の鎖数1
化学式量合計2951.50
構造登録者
主引用文献Cremonez, C.M.,Maiti, M.,Peigneur, S.,Cassoli, J.S.,Dutra, A.A.,Waelkens, E.,Lescrinier, E.,Herdewijn, P.,de Lima, M.E.,Pimenta, A.M.,Arantes, E.C.,Tytgat, J.
Structural and Functional Elucidation of Peptide Ts11 Shows Evidence of a Novel Subfamily of Scorpion Venom Toxins.
Toxins (Basel), 8:-, 2016
Cited by
PubMed Abstract: To date, several families of peptide toxins specifically interacting with ion channels in scorpion venom have been described. One of these families comprise peptide toxins (called KTxs), known to modulate potassium channels. Thus far, 202 KTxs have been reported, belonging to several subfamilies of KTxs (called α, β, γ, κ, δ, and λ-KTxs). Here we report on a previously described orphan toxin from venom, named Ts11. We carried out an in-depth structure-function analysis combining 3D structure elucidation of Ts11 and electrophysiological characterization of the toxin. The Ts11 structure is highlighted by an Inhibitor Cystine Knot (ICK) type scaffold, completely devoid of the classical secondary structure elements (α-helix and/or β-strand). This has, to the best of our knowledge, never been described before for scorpion toxins and therefore represents a novel, 6th type of structural fold for these scorpion peptides. On the basis of their preferred interaction with voltage-gated K channels, as compared to all the other targets tested, it can be postulated that Ts11 is the first member of a new subfamily, designated as ε-KTx.
PubMed: 27706049
DOI: 10.3390/toxins8100288
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2msf
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件を2026-01-21に公開中

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