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

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 (gD22–260: residues 22–260 and gD285: 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 gD285 has been purified and crystallized alone and in complex with HveA.