1L2G

Structure of a C-terminally truncated form of glycoprotein D from HSV-1

Summary for 1L2G

• Entry DOI: 10.2210/pdb1l2g/pdb
• Related: 1JMA
• Descriptor: Glycoprotein D, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: ig fold, viral envelope glycoprotein, viral protein
• Biological source: Human herpesvirus 1 (Herpes simplex virus type 1)
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P57083
• Total number of polymer chains: 4
• Total formula weight: 128233.50

Authors

Carfi, A.,Willis, S.H.,Whitbeck, J.C.,Krummenacher, C.,Cohen, G.H.,Eisenberg, R.J.,Wiley, D.C. (deposition date: 2002-02-21, release date: 2003-12-16, Last modification date: 2024-11-20)

Primary citation

Carfi, A.,Willis, S.H.,Whitbeck, J.C.,Krummenacher, C.,Cohen, G.H.,Eisenberg, R.J.,Wiley, D.C.
Herpes simplex virus glycoprotein D bound to the human receptor HveA.
Mol.Cell, 8:169-179, 2001

PubMed Abstract: 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.

PubMed: 11511370
DOI: 10.1016/S1097-2765(01)00298-2

Experimental method

X-RAY DIFFRACTION (2.85 Å)