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1jma
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(New page: 200px<br /> <applet load="1jma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jma, resolution 2.65Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:35, 12 November 2007
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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 with SO4 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
Page seeded by OCA on Mon Nov 12 17:42:23 2007
