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2gj7
From Proteopedia
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[[Image:2gj7.gif|left|200px]] | [[Image:2gj7.gif|left|200px]] | ||
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'''Crystal Structure of a gE-gI/Fc complex''' | '''Crystal Structure of a gE-gI/Fc complex''' | ||
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[[Category: Sprague, E R.]] | [[Category: Sprague, E R.]] | ||
[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:10:02 2008'' | |
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Revision as of 02:10, 4 May 2008
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 Page seeded by OCA on Sun May 4 05:10:02 2008
