Crystallization and preliminary diffraction studies of the ectodomain of the envelope glycoprotein D from herpes simplex virus 1 alone and in complex with the ectodomain of the human receptor HveA

被引:28
作者
Carfí, A
Gong, HY
Lou, H
Willis, SH
Cohen, GH
Eisenberg, RJ
Wiley, DC
机构
[1] Childrens Hosp, Dept Med, Boston, MA 02115 USA
[2] Howard Hughes Med Inst, Boston, MA 02115 USA
[3] Univ Penn, Sch Dent Med, Dept Microbiol, Philadelphia, PA 19104 USA
[4] Univ Penn, Sch Vet Med, Dept Pathobiol, Philadelphia, PA 19104 USA
[5] Harvard Univ, Howard Hughes Med Inst, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
D O I
10.1107/S0907444902001270
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Gycoprotein D (gD) is a glycoprotein expressed on the surface of several human and animal alpha herpes viruses. Binding of gD to cell-surface receptors has been shown to be necessary for herpes simplex virus 1 and 2 (HSV-1 and HSV-2) cell entry. The gD ectodomain consists of 316 residues and has no sequence homology to any other proteins of known structure. Two fragments of the HSV-1 gD ectodomain (gD(22-260): residues 22-260 and gD(285): residues 1-285) have been crystallized in two crystal forms. The complex between gD285 and the ectodomain of HveA, a gD cellular receptor member of the tumor necrosis factor (TNFR) superfamily, has also been crystallized. Moreover, insect-cell-expressed selenomethionine-substituted gD(285) has been purified and crystallized alone and in complex with HveA.
引用
收藏
页码:836 / 838
页数:3
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