2giy
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(New page: 200px<br /> <applet load="2giy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2giy, resolution 1.78Å" /> '''Crystal Structure o...)
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Revision as of 07:43, 18 November 2007
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Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain
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
2GIY is a Single protein structure of sequence from Human herpesvirus 4. 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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