Three-dimensional solution structure of the complex of α -bungarotoxin with a library-derived peptide

摘要

The solution structure of the complex be- tween α-bungarotoxin (α-BTX) and a 13-residue library- derived peptide (MRYYESSLKSYPD) has been solved using two-dimensional proton-NMR spectroscopy. The bound pep- tide adopts an almost-globular conformation resulting from three turns that surround a hydrophobic core formed by Tyr-11 of the peptide. The peptide fills an α-BTX pocket made of residues located at fingers I and II, as well as at the C-terminal region.