Crystal structure of glycoprotein B from herpes simplex virus 1

被引：465

作者：

Heldwein, Ekaterina E.

Lou, Huan

Bender, Florent C.

Cohen, Gary H.

Eisenberg, Roselyn J.

Harrison, Stephen C.

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[2] Childrens Hosp, Mol Med Lab, Boston, MA 02115 USA

[3] Childrens Hosp, Howard Hughes Med Inst, Boston, MA 02115 USA

[4] Univ Penn, Sch Dent Med, Dept Microbiol, Philadelphia, PA 19104 USA

[5] Univ Penn, Sch Vet Med, Dept Pathobiol, Philadelphia, PA 19104 USA

来源：

SCIENCE | 2006年 / 313卷 / 5784期

关键词：

D O I：

10.1126/science.1126548

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.

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页码：217 / 220

页数：4

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