Crystal structure of the principal neutralization site of HIV-1.
Science
; 264(5155): 82-5, 1994 Apr 01.
Article
en En
| MEDLINE
| ID: mdl-7511253
The crystal structure of a complex between a 24-amino acid peptide from the third variable (V3) loop of human immunodeficiency virus-type 1 (HIV-1) gp 120 and the Fab fragment of a broadly neutralizing antibody (59.1) was determined to 3 angstrom resolution. The tip of the V3 loop containing the Gly-Pro-Gly-Arg-Ala-Phe sequence adopts a double-turn conformation, which may be the basis of its conservation in many HIV-1 isolates. A complete map of the HIV-1 principal neutralizing determinant was constructed by stitching together structures of V3 loop peptides bound to 59.1 and to an isolate-specific (MN) neutralizing antibody (50.1). Structural conservation of the overlapping epitopes suggests that this biologically relevant conformation could be of use in the design of synthetic vaccines and drugs to inhibit HIV-1 entry and virus-related cellular fusion.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fragmentos de Péptidos
/
Fragmentos Fab de Inmunoglobulinas
/
Anticuerpos Anti-VIH
/
Proteína gp120 de Envoltorio del VIH
/
VIH-1
/
Complejo Antígeno-Anticuerpo
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Science
Año:
1994
Tipo del documento:
Article
Pais de publicación:
Estados Unidos