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Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILR?.


ABSTRACT: Paired Ig-like type 2 receptor ? (PILR?) 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 PILR?. Furthermore, we determined the crystal structures of PILR? and its complex with an sTn and its attached peptide region. The structures show that PILR? 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.

SUBMITTER: Kuroki K 

PROVIDER: S-EPMC4066494 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα.

Kuroki Kimiko K   Wang Jing J   Ose Toyoyuki T   Yamaguchi Munechika M   Tabata Shigekazu S   Maita Nobuo N   Nakamura Seiko S   Kajikawa Mizuho M   Kogure Amane A   Satoh Takeshi T   Arase Hisashi H   Maenaka Katsumi K  

Proceedings of the National Academy of Sciences of the United States of America 20140602 24


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 struc  ...[more]

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