1ZLC

Solution Conformation of alpha-conotoxin PIA

1ZLC の概要

• エントリーDOI: 10.2210/pdb1zlc/pdb
• NMR情報: BMRB: 6720
• 分子名称: Alpha-conotoxin PIA (1 entity in total)
• 機能のキーワード: alpha-helix, beta-turn, two disulfide bonds, c-terminal amidation, toxin
• 細胞内の位置: Secreted (By similarity): P69658
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1986.30

構造登録者

Chi, S.-W.,Lee, S.-H.,Kim, D.-H.,Kim, J.-S.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. (登録日: 2005-05-05, 公開日: 2006-05-02, 最終更新日: 2024-10-23)

主引用文献

Chi, S.-W.,Lee, S.-H.,Kim, D.-H.,Kim, J.-S.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H.
Solution structure of alpha-conotoxin PIA, a novel antagonist of alpha6 subunit containing nicotinic acetylcholine receptors
Biochem.Biophys.Res.Commun., 338:1990-1997, 2005

PubMed Abstract: alpha-Conotoxin PIA is a novel nicotinic acetylcholine receptor (nAChR) antagonist isolated from Conus purpurascens that targets nAChR subtypes containing alpha6 and alpha3 subunits. alpha-conotoxin PIA displays 75-fold higher affinity for rat alpha6/alpha3beta2beta3 nAChRs than for rat alpha3beta2 nAChRs. We have determined the three-dimensional structure of alpha-conotoxin PIA by nuclear magnetic resonance spectroscopy. The alpha-conotoxin PIA has an "omega-shaped" overall topology as other alpha4/7 subfamily conotoxins. Yet, unlike other neuronally targeted alpha4/7-conotoxins, its N-terminal tail Arg1-Asp2-Pro3 protrudes out of its main molecular body because Asp2-Pro3-Cys4-Cys5 forms a stable type I beta-turn. In addition, a kink introduced by Pro15 in the second loop of this toxin provides a distinct steric and electrostatic environment from those in alpha-conotoxins MII and GIC. By comparing the structure of alpha-conotoxin PIA with other functionally related alpha-conotoxins we suggest structural features in alpha-conotoxin PIA that may be associated with its unique receptor recognition profile.

PubMed: 16289101
DOI: 10.1016/j.bbrc.2005.10.176

実験手法

SOLUTION NMR