1D1H

SOLUTION STRUCTURE OF HANATOXIN 1

1D1H の概要

• エントリーDOI: 10.2210/pdb1d1h/pdb
• 分子名称: HANATOXIN TYPE 1 (1 entity in total)
• 機能のキーワード: cystine knot, toxin
• 由来する生物種: Grammostola rosea
• 細胞内の位置: Secreted: P56852
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4127.77

構造登録者

Takahashi, H.,Kim, J.I.,Sato, K.,Swartz, K.J.,Shimada, I. (登録日: 1999-09-16, 公開日: 2000-09-20, 最終更新日: 2024-10-30)

主引用文献

Takahashi, H.,Kim, J.I.,Min, H.J.,Sato, K.,Swartz, K.J.,Shimada, I.
Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins.
J.Mol.Biol., 297:771-780, 2000

PubMed Abstract: The three-dimensional structure of hanatoxin1 (HaTx1) was determined by using NMR spectroscopy. HaTx1 is a 35 amino acid residue peptide toxin that inhibits the drk1 voltage-gated K(+) channel not by blocking the pore, but by altering the energetics of gating. Both the amino acid sequence of HaTx1 and its unique mechanism of action distinguish this toxin from the previously described K(+) channel inhibitors. Unlike most other K(+) channel-blocking toxins, HaTx1 adopts an "inhibitor cystine knot" motif and is composed of two beta-strands, strand I for residues 19-21 and strand II for residues 28-30, connected by four chain reversals. A comparison of the surface features of HaTx1 with those of other gating modifier toxins of voltage-gated Ca(2+) and Na(+) channels suggests that the combination of a hydrophobic patch and surrounding charged residues is principally responsible for the binding of gating modifier toxins to voltage-gated ion channels.

PubMed: 10731427
DOI: 10.1006/jmbi.2000.3609

実験手法

SOLUTION NMR