Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics

BACKGROUND: α-Conotoxins have exciting therapeutic potential based on their high selectivity and affinity for nicotinic acetylcholine receptors. The spacing between the cysteine residues in α-conotoxins is variable, leading to the classification of sub-families. BuIA is the only α-conotoxin containi...

詳細記述

保存先:
書誌詳細
主要な著者: Jin, Ai-Hua, Brandstaetter, Hemma, Nevin, Simon T, Tan, Chia Chia, Clark, Richard J, Adams, David J, Alewood, Paul F, Craik, David J, Daly, Norelle L
フォーマット: 論文
言語:English
出版事項: BioMed Central 2007
主題:
Research Article
オンライン･アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1865545/
https://ncbi.nlm.nih.gov/pubmed/17445276
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1472-6807-7-28
タグ: タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!
id pubmed-1865545
record_format dspace
spelling pubmed-18655452007-05-05 Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics Jin, Ai-Hua Brandstaetter, Hemma Nevin, Simon T Tan, Chia Chia Clark, Richard J Adams, David J Alewood, Paul F Craik, David J Daly, Norelle L BMC Struct Biol Research Article BACKGROUND: α-Conotoxins have exciting therapeutic potential based on their high selectivity and affinity for nicotinic acetylcholine receptors. The spacing between the cysteine residues in α-conotoxins is variable, leading to the classification of sub-families. BuIA is the only α-conotoxin containing a 4/4 cysteine spacing and thus it is of significant interest to examine the structure of this conotoxin. RESULTS: In the current study we show the native globular disulfide connectivity of BuIA displays multiple conformations in solution whereas the non-native ribbon isomer has a single well-defined conformation. Despite having multiple conformations in solution the globular form of BuIA displays activity at the nicotinic acetylcholine receptor, contrasting with the lack of activity of the structurally well-defined ribbon isomer. CONCLUSION: These findings are opposite to the general trends observed for α-conotoxins where the native isomers have well-defined structures and the ribbon isomers are generally disordered. This study thus highlights the influence of the disulfide connectivity of BuIA on the dynamics of the three-dimensional structure. BioMed Central 2007-04-20 /pmc/articles/PMC1865545/ /pubmed/17445276 http://dx.doi.org/10.1186/1472-6807-7-28 Text en Copyright © 2007 Jin et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Research Article
spellingShingle Research Article
Jin, Ai-Hua
Brandstaetter, Hemma
Nevin, Simon T
Tan, Chia Chia
Clark, Richard J
Adams, David J
Alewood, Paul F
Craik, David J
Daly, Norelle L
Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
description BACKGROUND: α-Conotoxins have exciting therapeutic potential based on their high selectivity and affinity for nicotinic acetylcholine receptors. The spacing between the cysteine residues in α-conotoxins is variable, leading to the classification of sub-families. BuIA is the only α-conotoxin containing a 4/4 cysteine spacing and thus it is of significant interest to examine the structure of this conotoxin. RESULTS: In the current study we show the native globular disulfide connectivity of BuIA displays multiple conformations in solution whereas the non-native ribbon isomer has a single well-defined conformation. Despite having multiple conformations in solution the globular form of BuIA displays activity at the nicotinic acetylcholine receptor, contrasting with the lack of activity of the structurally well-defined ribbon isomer. CONCLUSION: These findings are opposite to the general trends observed for α-conotoxins where the native isomers have well-defined structures and the ribbon isomers are generally disordered. This study thus highlights the influence of the disulfide connectivity of BuIA on the dynamics of the three-dimensional structure.
author Jin, Ai-Hua
Brandstaetter, Hemma
Nevin, Simon T
Tan, Chia Chia
Clark, Richard J
Adams, David J
Alewood, Paul F
Craik, David J
Daly, Norelle L
author_facet Jin, Ai-Hua
Brandstaetter, Hemma
Nevin, Simon T
Tan, Chia Chia
Clark, Richard J
Adams, David J
Alewood, Paul F
Craik, David J
Daly, Norelle L
author_sort Jin, Ai-Hua
title Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
title_short Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
title_full Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
title_fullStr Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
title_full_unstemmed Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
title_sort structure of α-conotoxin buia: influences of disulfide connectivity on structural dynamics
publisher BioMed Central
publisher_facet BioMed Central
publishDate 2007
url https://ncbi.nlm.nih.gov/pmc/articles/PMC1865545/
https://ncbi.nlm.nih.gov/pubmed/17445276
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1472-6807-7-28
_version_ 1760479311779856384

類似資料