1MXP

Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB

1MXP の概要

• エントリーDOI: 10.2210/pdb1mxp/pdb
• 関連するPDBエントリー: 1MXN
• 分子名称: alpha-conotoxin AuIB (1 entity in total)
• 機能のキーワード: turns, toxin
• 細胞内の位置: Secreted: P56640
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1575.79

構造登録者

Dutton, J.L.,Bansal, P.S.,Hogg, R.C.,Adams, D.J.,Alewood, P.F.,Craik, D.J. (登録日: 2002-10-03, 公開日: 2002-12-30, 最終更新日: 2024-11-20)

主引用文献

Dutton, J.L.,Bansal, P.S.,Hogg, R.C.,Adams, D.J.,Alewood, P.F.,Craik, D.J.
A New Level of Conotoxin Diversity, a Non-native Disulfide Bond Connectivity in alpha -Conotoxin AuIB Reduces Structural Definition but Increases Biological Activity.
J.Biol.Chem., 277:48849-48857, 2002

PubMed Abstract: alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been synthesized to determine the role of disulfide bond connectivity on structure and activity. Both of these peptides contain the 15 amino acid sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the disulfide connectivity Cys(2-15 and 3-8). The solution structures of the peptides were determined by NMR spectroscopy, and their ability to block the nicotinic acetylcholine receptors on dissociated neurons of the rat parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to have approximately 10 times greater potency than the native peptide. To our knowledge this is the first demonstration of a non-native disulfide bond isomer of a conotoxin exhibiting greater biological activity than the native isomer.

PubMed: 12376538
DOI: 10.1074/jbc.M208842200

実験手法

SOLUTION NMR