3d2u | pdb_00003d2u

Structure of UL18, a Peptide-Binding Viral MHC Mimic, Bound to a Host Inhibitory Receptor

spinqualitylabelsall models 3d2u, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3d2u is a 8 chain structure with sequence from Homo sapiens and Human betaherpesvirus 5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.21Å Ligands: BMA, FUC, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UL18_HCMVA Plays a role in the protection against host NK cell cytotoxicity by interacting with and modulating the activity of the host inhibitory leukocyte Ig-like receptor 1/LILRB1, which is expressed on monocytes, dendritic cells, as well as subsets of T and NK cells. UL18 exerts an inhibitory effect on LIR-1+ NK cells, while it stimulates LIR-1- NK cell. These modulations prevent lysis of the infected cells by NK cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed UL18 is a human cytomegalovirus class I MHC (MHCI) homolog that binds the host inhibitory receptor LIR-1 and the only known viral MHC homolog that presents peptides. The 2.2-A structure of a LIR-1/UL18/peptide complex reveals increased contacts and optimal surface complementarity in the LIR-1/UL18 interface compared with LIR/MHCI interfaces, resulting in a >1,000-fold higher affinity. Despite sharing only approximately 25% sequence identity, UL18's structure and peptide binding are surprisingly similar to host MHCI. The crystal structure suggests that most of the UL18 surface, except where LIR-1 and the host-derived light chain bind, is covered by carbohydrates attached to 13 potential N-glycosylation sites, thereby preventing access to bound peptide and association with most MHCI-binding proteins. The LIR-1/UL18 structure demonstrates how a viral protein evolves from its host ancestor to impede unwanted interactions while preserving and improving its receptor-binding site. Structure of UL18, a peptide-binding viral MHC mimic, bound to a host inhibitory receptor.,Yang Z, Bjorkman PJ Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):10095-100. Epub 2008 Jul 15. PMID:18632577 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures Leukocyte immunoglobulin-like receptor

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