Solution structure of α-conotoxin PIA, a novel antagonist of α6 subunit containing nicotinic acetylcholine receptors =니코틴 아세틸콜린 수용체 알파6에 특이적 저해제인 알파코노톡신 PIA의 구조

Cited 11 time in scopus
Metadata Downloads
Title
Solution structure of α-conotoxin PIA, a novel antagonist of α6 subunit containing nicotinic acetylcholine receptors =니코틴 아세틸콜린 수용체 알파6에 특이적 저해제인 알파코노톡신 PIA의 구조
Author(s)
Seung-Wook Chi; Si-Hyung Lee; Do-Hyoung Kim; Jae Sung Kim; B M Olivera; J M McIntosh; Kyou Hoon Han
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 338, no. 4, pp. 1990-1997
Publication Year
2005
Abstract
α-Conotoxin PIA is a novel nicotinic acetylcholine receptor (nAChR) antagonist isolated from Conus purpurascens that targets nAChR subtypes containing α6 and α3 subunits. α-conotoxin PIA displays 75-fold higher affinity for rat α6/α3β2β3 nAChRs than for rat α3β2 nAChRs. We have determined the three-dimensional structure of α-conotoxin PIA by nuclear magnetic resonance spectroscopy. The α-conotoxin PIA has an "ω-shaped" overall topology as other α4/7 subfamily conotoxins. Yet, unlike other neuronally targeted α4/7-conotoxins, its N-terminal tail Arg1-Asp 2-Pro3 protrudes out of its main molecular body because Asp2-Pro3-Cys4-Cys5 forms a stable type I β-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 α-conotoxins MII and GIC. By comparing the structure of α-conotoxin PIA with other functionally related α-conotoxins we suggest structural features in α-conotoxin PIA that may be associated with its unique receptor recognition profile.
Keyword
α-conotoxinnicotinic acetylcholine receptorNMRpeptidesolution structure
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2005.10.176
Type
Article
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.