1998
Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding
Lentz T, Chaturvedi V, Conti-Fine B. Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding. Biochemical Pharmacology 1998, 55: 341-347. PMID: 9484801, DOI: 10.1016/s0006-2952(97)00474-7.Peer-Reviewed Original ResearchConceptsNicotine bindingCys-192Cys-193Alpha1 subunitReceptor alpha1 subunitReceptor α1 subunitTyr-190Tyr-198Acetylcholine receptorsΑ1 subunitGreater reductionAsp-195Significant reductionFusion proteinPro-194Single concentrationThr-196Apparent KdAmino acidsSynthetic peptidesAsp-200Position 181Individual amino acidsResidues 181Previous studies
1993
Effects of mutations of Torpedo acetylcholine receptor alpha 1 subunit residues 184-200 on alpha-bungarotoxin binding in a recombinant fusion protein.
Chaturvedi V, Donnelly-Roberts D, Lentz T. Effects of mutations of Torpedo acetylcholine receptor alpha 1 subunit residues 184-200 on alpha-bungarotoxin binding in a recombinant fusion protein. Biochemistry 1993, 32: 9570-6. PMID: 8373764, DOI: 10.1021/bi00088a008.Peer-Reviewed Original ResearchConceptsAlpha 1 subunitFusion proteinAlpha-bungarotoxin bindingFusion protein containingOligonucleotide-directed mutagenesisEffects of mutationsPossible structure-function relationshipsStructure-function relationshipsTyr-189Dissimilar residuesPro-194Recombinant fusion proteinHigher apparent affinityAlpha subunitTyr-198Asp-195Cys-192Cys-193Protein containingFunctional interactionAmino acidsSubunitsResiduesMutationsPosition 184