Journal
MOLECULAR CELL
Volume 8, Issue 1, Pages 169-179Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00298-2
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Funding
- NIAID NIH HHS [AI18289] Funding Source: Medline
- NINDS NIH HHS [NS30606, NS36731] Funding Source: Medline
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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 go both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another go receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin tig) fold at the core of go 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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