Acetylcholine interactions with tryptophan‐184 of the α‐subunit of the nicotinic acetylcholine receptor revealed by transferred nuclear Overhauser effect
- 21 October 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 291 (2) , 225-228
- https://doi.org/10.1016/0014-5793(91)81290-o
Abstract
Acetylcholine interactions with three genetically engineered fusion proteins containing peptides from the nicotinic acetylcholine receptor were studied by ID and 2D nuclear magnetic resonance methods. The three proteins were Torpedo α186–200, Torpedo α186–198, and human α183–204 of the acetylcholine receptor fused to the first 323 residues of the E. coli protein trpE. Nuclear Overhauser effect studies revealed interactions of bound acetylcholine with tryptophan-184 present in the Torpedo α184–200, and the human α183–204 sequences. These interactions are between the N(CH3)3+ and CH3 groups of acetylcholine with the aromatic protons of tryptophan. The appearance of these cross-peaks indicates a distance of less than 5 A between tryptophan and the bound ligand; however, direct contact has yet to be provenKeywords
This publication has 27 references indexed in Scilit:
- Structural determinants of .alpha.-bungarotoxin binding to the sequence segment 181-200 of the muscle nicotinic acetylcholine receptor .alpha. subunit: effects of cysteine/cystine modification and species-specific amino acid substitutionsBiochemistry, 1991
- Comparison of the toxin binding sites of the nicotinic acetylcholine receptor from Drosophila to humanBiochemistry, 1990
- Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxationBiochemistry, 1990
- Binding of .alpha.-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the .alpha. subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high-affinity binding by sodium dodecyl sulfateBiochemistry, 1988
- α‐Toxin binding to acetylcholine receptor α179–191 peptides: Intrinsic fluorescence studiesFEBS Letters, 1988
- Location of functional regions of acetylcholine receptor α-subunit by site-directed mutagenesisNature, 1985
- Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteinsJournal of Magnetic Resonance (1969), 1982
- Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spinsJournal of Magnetic Resonance (1969), 1981
- Structural study of the hydrophobic box region of lysozyme in solution using nuclear Overhauser effectsBiochemistry, 1980
- Acetylcholine Receptor: Covalent Attachment of Depolarizing Groups at the Active SiteScience, 1969