2giy: Difference between revisions
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[[Image:2giy.gif|left|200px]] | [[Image:2giy.gif|left|200px]] | ||
'''Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain''' | {{Structure | ||
|PDB= 2giy |SIZE=350|CAPTION= <scene name='initialview01'>2giy</scene>, resolution 1.78Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= GE, US8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 Human herpesvirus 4]) | |||
}} | |||
'''Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2GIY is a [ | 2GIY is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16646632 16646632] | ||
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral fc receptor]] | [[Category: viral fc receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:05:12 2008'' | ||
Revision as of 15:05, 20 March 2008
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| 2giy, resolution 1.78Å | |||||||||||||
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| Gene: | GE, US8 (Human herpesvirus 4) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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