1993/06/01 by Mauro Rustici, Luisa Bracci, Luisa Lozzi +5 · 5 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Immunology and Microbiology · #Acetylcholine #Acetylcholine receptor #Binding site #Biochemical and Structural Characterization #Biochemistry #Biology #Chemistry #Glycoprotein #Neurotoxin #Nicotinic acetylcholine receptor #Peptide #Pharmacology #Rabies #Rabies epidemiology and control #Rabies virus #Receptor #Stereochemistry #Tetrapeptide #Venomous Animal Envenomation and Studies #Virology #Virus
paper · doi:10.1002/bip.360330612
openalex publication_date 1993/06/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/26
The glycoprotein from the neurotropic rabies virus shows a significant homology with the alpha neurotoxin that binds to the nicotinic acetylcholine receptor. The crystal structure of the alpha neurotoxins suggests that the Arg 37 guanidinium group and the Asp 31 side-chain carboxylate of the erabutoxin have stereochemical features resembling those of acetylcholine. Conformational studies on the Asn194-Ser195-Arg196-Gly197 tetrapeptide, an essential part of the binding site of the rabies virus glycoprotein, indicate that the side chains of Asn and Arg could also mimic the acetylcholine structure. This observation is consistent with the recently proposed mechanism of the viral infection.