Structural highlights
Function
GD_HHV11 Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM, PVRL1 and 3-O-sulfated heparan sulfate (By similarity). May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL.
Publication Abstract from PubMed
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.
Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion.,Zhang N, Yan J, Lu G, Guo Z, Fan Z, Wang J, Shi Y, Qi J, Gao GF Nat Commun. 2011 Dec 6;2:577. doi: 10.1038/ncomms1571. PMID:22146396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang N, Yan J, Lu G, Guo Z, Fan Z, Wang J, Shi Y, Qi J, Gao GF. Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion. Nat Commun. 2011 Dec 6;2:577. doi: 10.1038/ncomms1571. PMID:22146396 doi:10.1038/ncomms1571
