1k64
From Proteopedia
|
NMR Structue of alpha-conotoxin EI
Overview
A high resolution structure of alpha-conotoxin EI has been determined by, (1)H NMR spectroscopy and molecular modeling. alpha-Conotoxin EI has the, same disulfide framework as alpha 4/7 conotoxins targeting neuronal, nicotinic acetylcholine receptors but antagonizes the neuromuscular, receptor as do the alpha 3/5 and alpha A conotoxins. The unique binding, preference of alpha-conotoxin EI to the alpha(1)/delta subunit interface, of Torpedo neuromuscular receptor makes it a valuable structural template, for superposition of various alpha-conotoxins possessing distinct receptor, subtype specificities. Structural comparison of alpha-conotoxin EI with, the gamma-subunit favoring alpha-conotoxin GI suggests that the Torpedo, delta-subunit preference of the former originates from its second loop., Superposition of three-dimensional structures of seven alpha-conotoxins, reveals that the estimated size of the toxin-binding pocket in nicotinic, acetylcholine receptor is approximately 20 A (height) x 20 A (width) x 15, A (thickness).
About this Structure
1K64 is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the alpha 1/delta subunit interface of torpedo nicotinic acetylcholine receptor., Park KH, Suk JE, Jacobsen R, Gray WR, McIntosh JM, Han KH, J Biol Chem. 2001 Dec 28;276(52):49028-33. Epub 2001 Oct 18. PMID:11641403
Page seeded by OCA on Tue Nov 20 18:53:08 2007
