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
1991
Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor.
Lentz T. Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor. Biochemistry 1991, 30: 10949-57. PMID: 1932020, DOI: 10.1021/bi00109a020.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding, CompetitiveCell MembraneElapid VenomsElectric OrganGlycoproteinsKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataNeurotoxinsPeptidesProtein ConformationRabies virusReceptors, NicotinicSequence Homology, Nucleic AcidTorpedoTubocurarineViral ProteinsConceptsRabies virus glycoproteinAcetylcholine receptorsVirus glycoproteinNicotinic acetylcholine receptorsTorpedo electric organ membranesElectric organ membranesD-tubocurarineToxin BReceptorsLoop 2Synthetic peptidesGlycoproteinPeptidesHigh affinityStructure-function relationshipsPhe-33GroupAcetylcholine