2GIY

Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain

Summary for 2GIY

• Entry DOI: 10.2210/pdb2giy/pdb
• Related: 2GJY
• Descriptor: Glycoprotein E (2 entities in total)
• Functional Keywords: viral fc receptor, ig v domain, viral protein
• Biological source: Human herpesvirus 1
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P04488
• Total number of polymer chains: 2
• Total formula weight: 42285.25

Authors

Sprague, E.R.,Wang, C.,Baker, D.,Bjorkman, P.J. (deposition date: 2006-03-29, release date: 2006-05-30, Last modification date: 2024-11-06)

Primary citation

Sprague, E.R.,Wang, C.,Baker, D.,Bjorkman, P.J.
Crystal Structure of the HSV-1 Fc Receptor Bound to Fc Reveals a Mechanism for Antibody Bipolar Bridging.
Plos Biol., 4:1-12, 2006

PubMed Abstract: 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.

PubMed: 16646632
DOI: 10.1371/journal.pbio.0040148

Experimental method

X-RAY DIFFRACTION (1.78 Å)