1l2g: Difference between revisions

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New page: left|200px<br /><applet load="1l2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2g, resolution 2.85Å" /> '''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"  
[[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==
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.
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==
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].  
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.]]
[[Category: Cohen, G.H.]]
[[Category: Cohen, G H.]]
[[Category: Eisenberg, R.J.]]
[[Category: Eisenberg, R J.]]
[[Category: Krummenacher, C.]]
[[Category: Krummenacher, C.]]
[[Category: Whitbeck, J.C.]]
[[Category: Whitbeck, J C.]]
[[Category: Wiley, D.C.]]
[[Category: Wiley, D C.]]
[[Category: Willis, S.H.]]
[[Category: Willis, S H.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: ig fold]]
[[Category: ig fold]]
[[Category: viral envelope glycoprotein]]
[[Category: viral envelope glycoprotein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:11:22 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:31 2008''