1jma: Difference between revisions

Revision as of 20:27, 1 July 2008

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File:1jma.png

Template:STRUCTURE 1jma

CRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEMCRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEM

Template:ABSTRACT PUBMED 11511370

About this StructureAbout this Structure

1JMA is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 1. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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+===CRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEM===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11511370}}, adds the Publication Abstract to the page
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 [[Category: Willis, S H.]]
 [[Category: V-type ig molecule and tnfr superfamily]]
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