2gj7
From Proteopedia
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| , resolution 5.Å | |||||||
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| Ligands: | , , , , | ||||||
| Gene: | IgG1 heavy chain (Homo sapiens), GE, US8 (Human herpesvirus 1) | ||||||
| Related: | 2GIY
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a gE-gI/Fc complex
Overview
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.
About this Structure
2GJ7 is a Protein complex structure of sequences from Cricetulus griseus, Homo sapiens and Human herpesvirus 1. Full crystallographic information is available from OCA.
Reference
Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging., Sprague ER, Wang C, Baker D, Bjorkman PJ, PLoS Biol. 2006 Jun;4(6):e148. Epub 2006 May 2. PMID:16646632
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