1K64

NMR Structue of alpha-conotoxin EI

1K64 の概要

• エントリーDOI: 10.2210/pdb1k64/pdb
• 関連するPDBエントリー: 1DG2 1PLP 1QS3
• 分子名称: alpha-conotoxin EI (1 entity in total)
• 機能のキーワード: omega-shaped containing a-helix, toxin
• 細胞内の位置: Secreted: P50982
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2098.41

構造登録者

Park, K.H.,Suk, J.E.,Jacobsen, R.,Gray, W.R.,McIntosh, J.M.,Han, K.H. (登録日: 2001-10-15, 公開日: 2003-09-09, 最終更新日: 2022-02-23)

主引用文献

Park, K.H.,Suk, J.E.,Jacobsen, R.,Gray, W.R.,McIntosh, J.M.,Han, K.H.
Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the alpha 1/delta subunit interface of torpedo nicotinic acetylcholine receptor
J.BIOL.CHEM., 276:49028-49033, 2001

PubMed Abstract: A high resolution structure of alpha-conotoxin EI has been determined by (1)H NMR spectroscopy and molecular modeling. alpha-Conotoxin EI has the same disulfide framework as alpha 4/7 conotoxins targeting neuronal nicotinic acetylcholine receptors but antagonizes the neuromuscular receptor as do the alpha 3/5 and alpha A conotoxins. The unique binding preference of alpha-conotoxin EI to the alpha(1)/delta subunit interface of Torpedo neuromuscular receptor makes it a valuable structural template for superposition of various alpha-conotoxins possessing distinct receptor subtype specificities. Structural comparison of alpha-conotoxin EI with the gamma-subunit favoring alpha-conotoxin GI suggests that the Torpedo delta-subunit preference of the former originates from its second loop. Superposition of three-dimensional structures of seven alpha-conotoxins reveals that the estimated size of the toxin-binding pocket in nicotinic acetylcholine receptor is approximately 20 A (height) x 20 A (width) x 15 A (thickness).

PubMed: 11641403
DOI: 10.1074/jbc.M107798200

実験手法

SOLUTION NMR