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1TYK

SOLUTION STRUCTURE OF A TOXIN FROM THE TARANTULA, GRAMMOSTOLA SPATULATA, WHICH INHIBITS MECHANOSENSITIVE ION CHANNELS

1LQR」から置き換えられました
1TYK の概要
エントリーDOI10.2210/pdb1tyk/pdb
関連するPDBエントリー1LQR
分子名称Toxin GsMTx-4 (1 entity in total)
機能のキーワードinhibitor, cysteine knot, beta-sheet, toxin
由来する生物種Grammostola rosea
細胞内の位置Secreted: Q7YT39
タンパク質・核酸の鎖数1
化学式量合計4109.93
構造登録者
Oswald, R.E.,Suchyna, T.M.,Mcfeeters, R.,Gottlieb, P.,Sachs, F. (登録日: 2004-07-08, 公開日: 2004-07-13, 最終更新日: 2024-11-13)
主引用文献Oswald, R.E.,Suchyna, T.M.,Mcfeeters, R.,Gottlieb, P.,Sachs, F.
Solution Structure of Peptide Toxins that Block Mechanosensitive Ion Channels
J.Biol.Chem., 277:34443-34450, 2002
Cited by
PubMed Abstract: Mechanosensitive channels (MSCs) play key roles in sensory processing and have been implicated as primary transducers for a variety of cellular responses ranging from osmosensing to gene expression. This paper presents the first structures of any kind known to interact specifically with MSCs. GsMTx-4 and GsMtx-2 are inhibitor cysteine knot peptides isolated from venom of the tarantula, Grammostola spatulata (Suchyna, T. M., Johnson, J. H., Hamer, K., Leykam, J. F., Gage, D. A., Clemo, H. F., Baumgarten, C. M., and Sachs, F. (2000) J. Gen. Physiol. 115, 583-598). Inhibition of cationic MSCs by the higher affinity GsMtx-4 (K(D) approximately 500 nm) reduced cell size in swollen and hypertrophic heart cells, swelling-activated currents in astrocytes, and stretch-induced arrhythmias in the heart. Despite the relatively low affinity, no cross-reactivity has been found with other channels. Using two-dimensional NMR spectroscopy, we determined the solution structure of GsMTx-4 and a lower affinity (GsMTx-2; K(D) approximately 6 microm) peptide from the same venom. The dominant feature of the two structures is a hydrophobic patch, utilizing most of the aromatic residues and surrounded with charged residues. The spatial arrangement of charged residues that are unique to GsMTx-4 and GsMTx-2 may underlie the selectivity of these peptides.
PubMed: 12082099
DOI: 10.1074/jbc.M202715200
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 1tyk
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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