2GCZ

Solution Structure of alpha-Conotoxin OmIA

2GCZ の概要

• エントリーDOI: 10.2210/pdb2gcz/pdb
• 分子名称: Alpha-conotoxin OmIA (1 entity in total)
• 機能のキーワード: alpha-helix, beta-turn, two disulfide bonds, c-terminal amidation, toxin
• 由来する生物種: Conus omaria (Omaria cone)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1725.97

構造登録者

Chi, S.-W.,Kim, D.-H.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. (登録日: 2006-03-15, 公開日: 2006-07-25, 最終更新日: 2020-06-24)

主引用文献

Chi, S.-W.,Kim, D.-H.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H.
Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes
Biochem.Biophys.Res.Commun., 345:248-254, 2006

PubMed Abstract: alpha-Conotoxin OmIA from Conus omaria is the only alpha-conotoxin that shows a approximately 20-fold higher affinity to the alpha3beta2 over the alpha6beta2 subtype of nicotinic acetylcholine receptor. We have determined a three-dimensional structure of alpha-conotoxin OmIA by nuclear magnetic resonance spectroscopy. alpha-Conotoxin OmIA has an "omega-shaped" overall topology with His(5)-Asn(12) forming an alpha-helix. Structural features of alpha-conotoxin OmIA responsible for its selectivity are suggested by comparing its surface characteristics with other functionally related alpha4/7 subfamily conotoxins. Reduced size of the hydrophilic area in alpha-conotoxin OmIA seems to be associated with the reduced affinity towards the alpha6beta2 nAChR subtype.

PubMed: 16678128
DOI: 10.1016/j.bbrc.2006.04.099

実験手法

SOLUTION NMR