3U82

Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion

Summary for 3U82

• Entry DOI: 10.2210/pdb3u82/pdb
• Related: 2C36 3ALP 3U83
• Descriptor: Envelope glycoprotein D, Poliovirus receptor-related protein 1 (2 entities in total)
• Functional Keywords: hsv-1 gd, nectin-1, binding mode, nectin-1 dimerization preclusion, viral protein-cell adhesion complex, viral protein/cell adhesion
• Biological source: Human herpesvirus 1 (HHV-1); More
• Cellular location: Virion membrane; Single-pass type I membrane protein (By similarity): Q69091; Isoform Alpha: Cell membrane; Single-pass type I membrane protein. Isoform Delta: Cell membrane; Single-pass type I membrane protein. Isoform Gamma: Secreted: Q15223
• Total number of polymer chains: 2
• Total formula weight: 67970.74

Authors

Zhang, N.,Yan, J.,Lu, G.,Guo, Z.,Fan, Z.,Wang, J.,Shi, Y.,Qi, J.,Gao, G.F. (deposition date: 2011-10-15, release date: 2012-03-21, Last modification date: 2024-11-20)

Primary citation

Zhang, N.,Yan, J.,Lu, G.,Guo, Z.,Fan, Z.,Wang, J.,Shi, Y.,Qi, J.,Gao, G.F.
Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion.
Nat Commun, 2:577-577, 2011

PubMed Abstract: Multiple surface envelope proteins are involved in the human herpes simplex virus type 1 entry and fusion. Among them, glycoprotein D (gD) has an important role by binding to the host receptors such as herpes virus entry mediator and nectin-1. Although the complex structure of gD with herpes virus entry mediator has been established, the binding mode of gD with the nectin-1 is elusive. Nectin-1 is a member of the immunoglobulin (Ig)-like (three Ig-like domains) cell adhesion molecules and is believed to form a homodimer to exert its functions. Here we report the complex structure of gD and nectin-1 (three Ig domains), revealing that gD binds the first Ig domain of nectin-1 in a similar mode to the nectin-1 homodimer interaction. The key amino acids responsible for nectin-1 dimerization are also used for gD/nectin-1 binding. This result indicates that binding of gD to nectin-1 would preclude the nectin-1 dimerization, consequently abolishing its cell adhesion function.

PubMed: 22146396
DOI: 10.1038/ncomms1571

Experimental method

X-RAY DIFFRACTION (3.164 Å)