2gj7
From Proteopedia
(New page: 200px<br /> <applet load="2gj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gj7, resolution 5.Å" /> '''Crystal Structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2gj7.gif|left|200px]]<br /> | + | [[Image:2gj7.gif|left|200px]]<br /><applet load="2gj7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2gj7" size=" | + | |
caption="2gj7, resolution 5.Å" /> | caption="2gj7, resolution 5.Å" /> | ||
'''Crystal Structure of a gE-gI/Fc complex'''<br /> | '''Crystal Structure of a gE-gI/Fc complex'''<br /> | ||
==Overview== | ==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 | + | 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== | ==About this Structure== | ||
| - | 2GJ7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | + | 2GJ7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJ7 OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Baker, D.]] | [[Category: Baker, D.]] | ||
| - | [[Category: Bjorkman, P | + | [[Category: Bjorkman, P J.]] |
| - | [[Category: Sprague, E | + | [[Category: Sprague, E R.]] |
[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
[[Category: fc receptor]] | [[Category: fc receptor]] | ||
[[Category: low resolution]] | [[Category: low resolution]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:12 2008'' |
Revision as of 15:32, 21 February 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 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
Page seeded by OCA on Thu Feb 21 17:32:12 2008
