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

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

SUBMITTER: Jin AH 

PROVIDER: S-EPMC1865545 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature