Structural highlights
3u82 is a 2 chain structure with sequence from Hhv-1 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 2c36, 3alp, 3u83 |
| Gene: | gD, US6 (HHV-1), PVRL1, HVEC, PRR1 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
[PVRL1_HUMAN] Zlotogora-Ogur syndrome;Cleft lip with or without cleft palate. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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. [PVRL1_HUMAN] Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4. Functions as an entry receptor for herpes simplex virus and pseudorabies virus.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lopez M, Eberle F, Mattei MG, Gabert J, Birg F, Bardin F, Maroc C, Dubreuil P. Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene. Gene. 1995 Apr 3;155(2):261-5. PMID:7721102
- ↑ 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
