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BMC Struct Biol. 2007 Apr 20;7:28.

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

Author information

1
Institute for Molecular Bioscience, Australian Research Council Special Research Centre for Functional and Applied Genomics, The University of Queensland, Brisbane QLD, Australia. a.jin@imb.uq.edu.au <a.jin@imb.uq.edu.au>

Abstract

BACKGROUND:

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

PMID:
17445276
PMCID:
PMC1865545
DOI:
10.1186/1472-6807-7-28
[Indexed for MEDLINE]
Free PMC Article

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