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 1.78&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain'''<br />
'''Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain'''<br />
==Overview==
==Overview==
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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.
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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==
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2GIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GIY OCA].
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2GIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [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=2GIY OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baker, D.]]
[[Category: Baker, D.]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Sprague, E.R.]]
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[[Category: Sprague, E R.]]
[[Category: Wang, C.]]
[[Category: Wang, C.]]
[[Category: ig v domain]]
[[Category: ig v domain]]
[[Category: viral fc receptor]]
[[Category: viral fc receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:50:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:08 2008''

Revision as of 15:32, 21 February 2008


2giy, resolution 1.78Å

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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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