Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2LO7

Ts16 NMR solution structure

2LKA」から置き換えられました
2LO7 の概要
エントリーDOI10.2210/pdb2lo7/pdb
NMR情報BMRB: 17987
分子名称Toxin Ts16 (1 entity in total)
機能のキーワードcs alpha alpha motif, alpha scorpion toxin, voltage gated potassium channel, toxin
由来する生物種Tityus serrulatus (Brazilian scorpion)
細胞内の位置Secreted: P86271
タンパク質・核酸の鎖数1
化学式量合計3460.13
構造登録者
del Rio-Portilla, F.,Saucedo, A.L.,Flores-Solis, D. (登録日: 2012-01-17, 公開日: 2012-03-14, 最終更新日: 2024-11-20)
主引用文献Saucedo, A.L.,Flores-Solis, D.,Rodriguez de la Vega, R.C.,Ramirez-Cordero, B.,Hernandez-Lopez, R.,Cano-Sanchez, P.,Navarro, R.N.,Garcia-Valdes, J.,Coronas-Valderrama, F.,de Roodt, A.,Brieba, L.G.,Possani, L.D.,Del Rio-Portilla, F.
New Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACING.
J.Biol.Chem., 287:12321-12330, 2012
Cited by
PubMed Abstract: Scorpion venoms are a rich source of K(+) channel-blocking peptides. For the most part, they are structurally related small disulfide-rich proteins containing a conserved pattern of six cysteines that is assumed to dictate their common three-dimensional folding. In the conventional pattern, two disulfide bridges connect an α-helical segment to the C-terminal strand of a double- or triple-stranded β-sheet, conforming a cystine-stabilized α/β scaffold (CSα/β). Here we show that two K(+) channel-blocking peptides from Tityus scorpions conserve the cysteine spacing of common scorpion venom peptides but display an unconventional disulfide pattern, accompanied by a complete rearrangement of the secondary structure topology into a CS helix-loop-helix fold. Sequence and structural comparisons of the peptides adopting this novel fold suggest that it would be a new elaboration of the widespread CSα/β scaffold, thus revealing an unexpected structural versatility of these small disulfide-rich proteins. Acknowledgment of such versatility is important to understand how venom structural complexity emerged on a limited number of molecular scaffolds.
PubMed: 22238341
DOI: 10.1074/jbc.M111.329607
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 2lo7
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

PDB statisticsPDBj update infoContact PDBjnumon