Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3965
Title: A model of the rabies virus glycoprotein active site
Authors: Rustici, M.
Bracci, Luisa
Lozzi, Luisa
Neri, Paolo
Santucci, Annalisa 
Soldani, Patrizia 
Spreafico, Adriano
Niccolai, Neri 
Issue Date: 1993
Project: None 
Journal: BIOPOLYMERS
Abstract: 
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.
Description: 
36432
URI: http://hdl.handle.net/20.500.12779/3965
ISSN: 0006-3525
DOI: 10.1002/bip.360330612
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.