A model of the rabies virus glycoprotein active site.
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.
Rustici
M
M
Dipartimento di Biologia Molecolare Università di Siena, Italia.
Bracci
L
L
Lozzi
L
L
Neri
P
P
Santucci
A
A
Soldani
P
P
Spreafico
A
A
Niccolai
N
N
D000595:Amino Acid Sequence; D000956:Antigens, Viral; D001665:Binding Sites; D003198:Computer Simulation; D006023:Glycoproteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011820:Rabies virus; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000737:chemistry*
D000956:Antigens, Viral; D006023:Glycoproteins; D014759:Viral Envelope Proteins; C064951:glycoprotein G, Rabies virus