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1jma
From Proteopedia
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[[Image:1jma.gif|left|200px]] | [[Image:1jma.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEM''' | '''CRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEM''' | ||
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[[Category: Wiley, D C.]] | [[Category: Wiley, D C.]] | ||
[[Category: Willis, S H.]] | [[Category: Willis, S H.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:24:01 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:24, 2 May 2008
CRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEM
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
1JMA is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 1. 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 Page seeded by OCA on Fri May 2 21:24:01 2008
