3wv0 | pdb_00003wv0

O-glycan attached to herpes simplex virus type 1 glycoprotein gB is recognized by the Ig V-set domain of human paired immunoglobulin-like type 2 receptor alpha

spinqualitylabelsall models 3wv0, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wv0 is a 4 chain structure with sequence from Homo sapiens and Human alphaherpesvirus 1 strain KOS. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: A2G, SIA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PILRA_HUMAN Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP. Publication Abstract from PubMed Paired Ig-like type 2 receptor alpha (PILRalpha) recognizes a wide range of O-glycosylated mucin and related proteins to regulate broad immune responses. However, the molecular characteristics of these recognitions are largely unknown. Here we show that sialylated O-linked sugar T antigen (sTn) and its attached peptide region are both required for ligand recognition by PILRalpha. Furthermore, we determined the crystal structures of PILRalpha and its complex with an sTn and its attached peptide region. The structures show that PILRalpha exhibits large conformational change to recognize simultaneously both the sTn O-glycan and the compact peptide structure constrained by proline residues. Binding and functional assays support this binding mode. These findings provide significant insight into the binding motif and molecular mechanism (which is distinct from sugar-recognition receptors) by which O-glycosylated mucin proteins with sTn modifications are recognized in the immune system as well as during viral entry. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRalpha.,Kuroki K, Wang J, Ose T, Yamaguchi M, Tabata S, Maita N, Nakamura S, Kajikawa M, Kogure A, Satoh T, Arase H, Maenaka K Proc Natl Acad Sci U S A. 2014 Jun 17;111(24):8877-82. doi:, 10.1073/pnas.1324105111. Epub 2014 Jun 2. PMID:24889612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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