Binding mode of alpha-conotoxins to an acetylcholine binding protein determined by saturation transfer difference NMR

Westermann, Jan, Clark, Richard J. and Craik, David J. (2008) Binding mode of alpha-conotoxins to an acetylcholine binding protein determined by saturation transfer difference NMR. Protein And Peptide Letters, 15 9: 910-914. doi:10.2174/092986608785849335


Author Westermann, Jan
Clark, Richard J.
Craik, David J.
Title Binding mode of alpha-conotoxins to an acetylcholine binding protein determined by saturation transfer difference NMR
Formatted title
Binding Mode of α-Conotoxins to an Acetylcholine Binding Protein Determined by Saturation Transfer Difference NMR
Journal name Protein And Peptide Letters   Check publisher's open access policy
ISSN 0929-8665
1875-5305
Publication date 2008-05-01
Year available 2008
Sub-type Article (original research)
DOI 10.2174/092986608785849335
Open Access Status
Volume 15
Issue 9
Start page 910
End page 914
Total pages 5
Editor Ben M. Dunn
Place of publication Schiphol, The Netherlands
Publisher Bentham Science Publishers
Language eng
Subject C1
030406 Proteins and Peptides
970103 Expanding Knowledge in the Chemical Sciences
Abstract The saturation transfer difference (STD) NMR technique was employed to study the complex of the alpha-conotoxins Vc1.1 and MII bound to the acetylcholine binding protein (AChBP) from Lymnea stagnalis, a model system of the 7 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 alpha-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.
Formatted abstract
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.
Keyword Proteins
Binding proteins
Alpha-conotoxin
Acetylcholine binding protein
Saturation transfer
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Thu, 16 Apr 2009, 01:07:49 EST by Jennifer Greder on behalf of Institute for Molecular Bioscience