2ns3 | pdb_00002ns3
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Solution structure of ribbon BuIA
Overview
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.
About this Structure
2NS3 is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Structure of alpha-conotoxin BuIA: influences of disulfide connectivity on structural dynamics., Jin AH, Brandstaetter H, Nevin ST, Tan CC, Clark RJ, Adams DJ, Alewood PF, Craik DJ, Daly NL, BMC Struct Biol. 2007 Apr 20;7:28. PMID:17445276
Page seeded by OCA on Wed Jan 23 13:26:44 2008
