2GIY: Crystal Structure Of The C-terminal Domain Of The Hsv-1 Ge Ectodomain

Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releases it at the acidic pH of lysosomes, consistent with a role in facilitating the degradation of antiviral antibodies. Here we identify the C-terminal domain of the gE ectodomain (CgE) as the minimal Fc-binding domain and present a 1.78-angstroms CgE structure. A 5-angstroms gE-gI/Fc crystal structure, which was independently verified by a theoretical prediction method, reveals that CgE binds Fc at the C(H)2-C(H)3 interface, the binding site for several mammalian and bacterial Fc-binding proteins. The structure identifies interface histidines that may confer pH-dependent binding and regions of CgE implicated in cell-to-cell spread of virus. The ternary organization of the gE-gI/Fc complex is compatible with antibody bipolar bridging, which can interfere with the antiviral immune response.
PDB ID: 2GIYDownload
MMDB ID: 39379
PDB Deposition Date: 2006/3/29
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.78  Å
Source Organism:
Similar Structures:
Biological Unit for 2GIY: dimeric; determined by author and by software (PISA)
Molecular Components in 2GIY
Label Count Molecule
Proteins (2 molecules)
Glycoprotein E
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB