3u83 | pdb_00003u83

Crystal structure of nectin-1

spinqualitylabelsall models 3u83, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 Isolated cleft lip;Cleft lip/palate-ectodermal dysplasia syndrome;Cleft lip and alveolus;Cleft lip/palate. 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. (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Poliovirus receptor-related protein

Proteopedia Page Contributors and Editors (what is this?)

OCA