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Binding Mode of α-Conotoxins to an Acetylcholine Binding Protein Determined by Saturation Transfer Difference NMR

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The saturation transfer difference (STD) NMR technique was employed to study the complex of the α-conotoxins Vc1.1 and MII bound to the acetylcholine binding protein (AChBP) from Lymnea stagnalis, a model system of the α7 subunit of the nicotinic acetylcholine receptor. MII was found to be the more potent ligand for AChBP, consistent with data from electrophysiology measurements for the nicotinic acetylcholine receptor. Both peptides displayed strong interactions on aromatic residues in the α-helical part of their sequences, i.e., Tyr10 in Vc1.1 and His9 in MII respectively. From the STD NMR spectra it was determined that the peptides are buried in the nicotinic binding site of ACBP as has been previously shown for the conotoxins PnIA[A10L, D14K], ImI and TxIA[A10L] by X-ray crystallography. This study demonstrates the value of STD NMR in the study of conotoxin binding to receptor proteins.

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Keywords: AChBP; Conotoxin; STD NMR; binding; nAChR

Document Type: Research Article

Publication date: 01 September 2008

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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