1mxp
From Proteopedia
Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB
Overview
alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been synthesized to determine the role of disulfide bond connectivity on structure and activity. Both of these peptides contain the 15 amino acid sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the disulfide connectivity Cys(2-15 and 3-8). The solution structures of the peptides were determined by NMR spectroscopy, and their ability to block the nicotinic acetylcholine receptors on dissociated neurons of the rat parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to have approximately 10 times greater potency than the native peptide. To our knowledge this is the first demonstration of a non-native disulfide bond isomer of a conotoxin exhibiting greater biological activity than the native isomer.
About this Structure
1MXP is a Single protein structure. Full crystallographic information is available from OCA.
Reference
A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity., Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ, J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:12376538 Page seeded by OCA on Sat May 3 01:50:44 2008
