3WV0
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
Summary for 3WV0
| Entry DOI | 10.2210/pdb3wv0/pdb |
| Related | 3WUZ |
| Descriptor | Paired immunoglobulin-like type 2 receptor alpha, Envelope glycoprotein B, N-acetyl-alpha-neuraminic acid-(2-6)-2-acetamido-2-deoxy-alpha-D-galactopyranose, ... (5 entities in total) |
| Functional Keywords | immunoglobulin-like, immunological receptor, membrane, membrane protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Virion membrane ; Single-pass type I membrane protein : P06437 |
| Total number of polymer chains | 4 |
| Total formula weight | 30948.17 |
| Authors | Kuroki, K.,Wang, J.,Ose, T.,Yamaguchi, M.,Tabata, S.,Maita, N.,Nakamura, S.,Kajikawa, M.,Kogure, A.,Satoh, T.,Arase, H.,Maenaka, K. (deposition date: 2014-05-10, release date: 2014-06-11, Last modification date: 2024-11-20) |
| Primary citation | Kuroki, K.,Wang, J.,Ose, T.,Yamaguchi, M.,Tabata, S.,Maita, N.,Nakamura, S.,Kajikawa, M.,Kogure, A.,Satoh, T.,Arase, H.,Maenaka, K. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILR alpha Proc.Natl.Acad.Sci.USA, 111:8877-8882, 2014 Cited by PubMed Abstract: Paired Ig-like type 2 receptor α (PILRα) 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 PILRα. Furthermore, we determined the crystal structures of PILRα and its complex with an sTn and its attached peptide region. The structures show that PILRα 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. PubMed: 24889612DOI: 10.1073/pnas.1324105111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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