3u83

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Crystal structure of nectin-1

Structural highlights

3u83 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.499Å
Ligands:PG6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

NECT1_HUMAN Cleft lip/palate;Isolated cleft lip;Cleft lip and alveolus;Cleft lip/palate-ectodermal dysplasia syndrome. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

NECT1_HUMAN Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some neurite outgrowth-promoting activity.[1] (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV.[2] [3]

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[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
16 reviews cite this structure
Herpes virus fusion and entry: a story with many characters.
Eisenberg et al. (2012)
15 more
44 other articles
No citations found

See Also

References

  1. ↑ Di Giovine P, Settembre EC, Bhargava AK, Luftig MA, Lou H, Cohen GH, Eisenberg RJ, Krummenacher C, Carfi A. Structure of herpes simplex virus glycoprotein d bound to the human receptor nectin-1. PLoS Pathog. 2011 Sep;7(9):e1002277. Epub 2011 Sep 29. PMID:21980294 doi:10.1371/journal.ppat.1002277
  2. ↑ 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
  3. ↑ Warner MS, Geraghty RJ, Martinez WM, Montgomery RI, Whitbeck JC, Xu R, Eisenberg RJ, Cohen GH, Spear PG. A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus. Virology. 1998 Jun 20;246(1):179-89. PMID:9657005 doi:http://dx.doi.org/10.1006/viro.1998.9218
  4. ↑ 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

Contents


PDB ID 3u83

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