1l2g
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| , resolution 2.85Å | |||||||
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| Ligands: | |||||||
| Related: | 1JMA
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a C-terminally truncated form of glycoprotein D from HSV-1
OverviewOverview
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 StructureAbout this Structure
1L2G is a Single protein structure of sequence from 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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