1l2g

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(New page: 200px<br /><applet load="1l2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2g, resolution 2.85&Aring;" /> '''Structure of a C-ter...)
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[[Image:1l2g.jpg|left|200px]]<br /><applet load="1l2g" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l2g.jpg|left|200px]]<br /><applet load="1l2g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l2g, resolution 2.85&Aring;" />
caption="1l2g, resolution 2.85&Aring;" />
'''Structure of a C-terminally truncated form of glycoprotein D from HSV-1'''<br />
'''Structure of a C-terminally truncated form of glycoprotein D from HSV-1'''<br />
==Overview==
==Overview==
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Herpes simplex virus (HSV) infection requires binding of the viral, envelope glycoprotein D (gD) to cell surface receptors. We report the, X-ray structures of a soluble, truncated ectodomain of gD both alone and, in complex with the ectodomain of its cellular receptor HveA. Two bound, anions suggest possible binding sites for another gD receptor, a, 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a, V-like immunoglobulin (Ig) fold at the core of gD that is closely related, to cellular adhesion molecules and flanked by large N- and C-terminal, extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change, accompanying binding might be part of the viral entry mechanism.
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Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of gD both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the core of gD that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.
==About this Structure==
==About this Structure==
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1L2G 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L2G OCA].
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1L2G 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=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2G OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carfi, A.]]
[[Category: Carfi, A.]]
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[[Category: Cohen, G.H.]]
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[[Category: Cohen, G H.]]
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[[Category: Eisenberg, R.J.]]
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[[Category: Eisenberg, R J.]]
[[Category: Krummenacher, C.]]
[[Category: Krummenacher, C.]]
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[[Category: Whitbeck, J.C.]]
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[[Category: Whitbeck, J C.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
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[[Category: Willis, S.H.]]
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[[Category: Willis, S H.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: ig fold]]
[[Category: ig fold]]
[[Category: viral envelope glycoprotein]]
[[Category: viral envelope glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:11:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:31 2008''

Revision as of 11:40, 21 February 2008


1l2g, resolution 2.85Å

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Structure of a C-terminally truncated form of glycoprotein D from HSV-1

Overview

Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of gD both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the core of gD that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.

About this Structure

1L2G is a Single protein structure of sequence from Human herpesvirus 4 with as ligand. Full crystallographic information is available from OCA.

Reference

Herpes simplex virus glycoprotein D bound to the human receptor HveA., Carfi A, Willis SH, Whitbeck JC, Krummenacher C, Cohen GH, Eisenberg RJ, Wiley DC, Mol Cell. 2001 Jul;8(1):169-79. PMID:11511370

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