High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding.
EMBO J
; 16(16): 5139-48, 1997 Aug 15.
Article
en En
| MEDLINE
| ID: mdl-9305654
ABSTRACT
The crystal structure of a recombinant polyomavirus VP1 pentamer (residues 32-320) in complex with a branched disialylated hexasaccharide receptor fragment has been determined at 1.9 A resolution. The result extends our understanding of oligosaccharide receptor recognition. It also suggests a mechanism for enhancing the fidelity of virus assembly. We have previously described the structure of the complete polyomavirus particle complexed with this receptor fragment at 3.65 A. The model presented here offers a much more refined view of the interactions that determine carbohydrate recognition and allows us to assign additional specific contacts, in particular those involving the (alpha2,6)-linked, branching sialic acid. The structure of the unliganded VP1 pentamer, determined independently, shows that the oligosaccharide fits into a preformed groove and induces no measurable structural rearrangements. A comparison with assembled VP1 in the virus capsid reveals a rearrangement of residues 32-45 at the base of the pentamer. This segment may help prevent the formation of incorrectly assembled particles by reducing the likelihood that the C-terminal arm will fold back into its pentamer of origin.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Oligosacáridos
/
Receptores Virales
/
Cápside
/
Poliomavirus
/
Ensamble de Virus
/
Proteínas de la Cápside
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
EMBO J
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos