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PDBsum entry 3wuz
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Membrane protein
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PDB id
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3wuz
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PDB id:
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| Name: |
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Membrane protein
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Title:
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Crystal structure of the ig v-set domain of human paired immunoglobulin-like type 2 receptor alpha
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Structure:
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Paired immunoglobulin-like type 2 receptor alpha. Chain: a. Fragment: v-set domain, unp residues 32-150. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: pilra. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.30Å
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R-factor:
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0.146
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R-free:
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0.178
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Authors:
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K.Kuroki,J.Wang,T.Ose,M.Yamaguchi,S.Tabata,N.Maita,S.Nakamura, M.Kajikawa,A.Kogure,T.Satoh,H.Arase,K.Maenaka
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Key ref:
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K.Kuroki
et al.
(2014).
Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα.
Proc Natl Acad Sci U S A,
111,
8877-8882.
PubMed id:
DOI:
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Date:
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10-May-14
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Release date:
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11-Jun-14
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PROCHECK
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Headers
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References
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Q9UKJ1
(PILRA_HUMAN) -
Paired immunoglobulin-like type 2 receptor alpha from Homo sapiens
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Seq:
Struc:
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303 a.a.
120 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Proc Natl Acad Sci U S A
111:8877-8882
(2014)
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PubMed id:
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Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα.
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K.Kuroki,
J.Wang,
T.Ose,
M.Yamaguchi,
S.Tabata,
N.Maita,
S.Nakamura,
M.Kajikawa,
A.Kogure,
T.Satoh,
H.Arase,
K.Maenaka.
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ABSTRACT
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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.
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Links
