2gum
From Proteopedia
(New page: 200px<br /><applet load="2gum" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gum, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:2gum.gif|left|200px]]<br /><applet load="2gum" size=" | + | [[Image:2gum.gif|left|200px]]<br /><applet load="2gum" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gum, resolution 2.10Å" /> | caption="2gum, resolution 2.10Å" /> | ||
'''Crystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I'''<br /> | '''Crystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glycoprotein B (gB) is the most conserved component of the complex | + | Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes. |
==About this Structure== | ==About this Structure== | ||
| - | 2GUM 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] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2GUM 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] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GUM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Heldwein, E | + | [[Category: Heldwein, E E.]] |
[[Category: NA]] | [[Category: NA]] | ||
[[Category: envelope glycoprotein]] | [[Category: envelope glycoprotein]] | ||
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[[Category: virus]] | [[Category: virus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:35:32 2008'' |
Revision as of 15:35, 21 February 2008
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Crystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I
Overview
Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.
About this Structure
2GUM is a Single protein structure of sequence from Human herpesvirus 4 with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of glycoprotein B from herpes simplex virus 1., Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, Harrison SC, Science. 2006 Jul 14;313(5784):217-20. PMID:16840698
Page seeded by OCA on Thu Feb 21 17:35:32 2008
