1BKT
BMKTX TOXIN FROM SCORPION BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES
1BKT の概要
エントリーDOI | 10.2210/pdb1bkt/pdb |
分子名称 | BMKTX (1 entity in total) |
機能のキーワード | scorpion, neurotoxin, large conductance potassium channel, voltage gated potassium channel, buthus martensii |
由来する生物種 | Mesobuthus martensii (Chinese scorpion) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 3975.84 |
構造登録者 | Renisio, J.G.,Romi-Lebrun, R.,Blanc, E.,Bornet, O.,Nakajima, T.,Darbon, H. (登録日: 1998-07-03, 公開日: 1999-01-13, 最終更新日: 2024-10-23) |
主引用文献 | Renisio, J.G.,Romi-Lebrun, R.,Blanc, E.,Bornet, O.,Nakajima, T.,Darbon, H. Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi Proteins, 38:70-78, 2000 Cited by PubMed Abstract: BmKTX is a toxin recently purified from the venom of Buthus Martensi, which belongs to the kaliotoxin family. We have determined its solution structure by use of conventional two-dimensional NMR techniques followed by distance-geometry and energy minimization. The calculated structure is composed of a short alpha-helix (residues 14 to 20) connected by a tight turn to a two-stranded antiparallel beta-sheet (sequences 25-27 and 32-34). The beta-turn connecting these strands belongs to type I. The N-terminal segment (sequence 1 to 8) runs parallel to the beta-sheet although it cannot be considered as a third strand. Comparison of the conformation of BmKTX and toxins of the kaliotoxin family clearly demonstrates that they are highly related. Therefore, analysis of the residues belonging to the interacting surface of those toxins allows us to propose a functional map of BmKTX slightly different from the one of KTX and AgTX2, which may explain the variations in affinities of these toxins towards the Kv1.3 channels. PubMed: 10651040DOI: 10.1002/(SICI)1097-0134(20000101)38:1<70::AID-PROT8>3.0.CO;2-5 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
検証レポート(詳細版)をダウンロード