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Titolo:
Herpes simplex virus glycoprotein D bound to the human receptor HveA
Autore:
Carfi, A; Willis, SH; Whitbeck, JC; Krummenacher, C; Cohen, GH; Eisenberg, RJ; Wiley, DC;
Indirizzi:
Howard Hughes Med Inst, Childrens Hosp, Dept Med, Boston, MA 02115 USA Howard Hughes Med Inst Boston MA USA 02115 Dept Med, Boston, MA 02115 USA Harvard Univ, Howard Hughes Med Inst, Dept Mol & Cellular Biol, Cambridge,MA 02138 USA Harvard Univ Cambridge MA USA 02138 Cellular Biol, Cambridge,MA 02138 USA Univ Penn, Sch Vet Med, Dept Pathobiol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Pathobiol, Philadelphia, PA 19104 USA Univ Penn, Sch Dent Med, Dept Microbiol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Microbiol, Philadelphia, PA 19104 USA
Titolo Testata:
MOLECULAR CELL
fascicolo: 1, volume: 8, anno: 2001,
pagine: 169 - 179
SICI:
1097-2765(200107)8:1<169:HSVGDB>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
NECROSIS-FACTOR RECEPTOR; CELL-SURFACE RECEPTORS; ENTRY MEDIATOR; MONOCLONAL-ANTIBODIES; POLIOVIRUS RECEPTOR; CRYSTAL-STRUCTURE; HEPARAN-SULFATE; SOLUBLE FORM; BINDING; TYPE-1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Wiley, DC Howard Hughes Med Inst, Childrens Hosp, Dept Med, 320 Longwood Ave, Boston, MA 02115 USA Howard Hughes Med Inst 320 Longwood Ave Boston MA USA 02115 USA
Citazione:
A. Carfi et al., "Herpes simplex virus glycoprotein D bound to the human receptor HveA", MOL CELL, 8(1), 2001, pp. 169-179

Abstract

Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of go both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another go receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin tig) fold at the core of go that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 02:04:54