5XO2

Crystal structure of human paired immunoglobulin-like type 2 receptor alpha with synthesized glycopeptide II


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.229 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILR alpha immune cell receptor.

Furukawa, A.Kakita, K.Yamada, T.Ishizuka, M.Sakamoto, J.Hatori, N.Maeda, N.Ohsaka, F.Saitoh, T.Nomura, T.Kuroki, K.Nambu, H.Arase, H.Matsunaga, S.Anada, M.Ose, T.Hashimoto, S.Maenaka, K.

(2017) J Biol Chem 292: 21128-21136

  • DOI: https://doi.org/10.1074/jbc.M117.799239
  • Primary Citation of Related Structures:  
    5XO2, 5XOF

  • PubMed Abstract: 

    Before entering host cells, herpes simplex virus-1 uses its envelope glycoprotein B to bind paired immunoglobulin-like type 2 receptor α (PILRα) on immune cells. PILRα belongs to the Siglec (sialic acid (SA)-binding immunoglobulin-like lectin)-like family, members of which bind SA. PILRα is the only Siglec member to recognize not only the sialylated O -linked sugar T antigen (sTn) but also its attached peptide region. We previously determined the crystal structure of PILRα complexed with the sTn-linked glycopeptide of glycoprotein B, revealing the simultaneous recognition of sTn and peptide by the receptor. However, the contribution of each glycopeptide component to PILRα binding was largely unclear. Here, we chemically synthesized glycopeptide derivatives and determined the thermodynamic parameters of their interaction with PILRα. We show that glycopeptides with different sugar units linking SA and peptides ( i.e. "GlcNAc-type" and "deoxy-GlcNAc-type" glycopeptides) have lower affinity and more enthalpy-driven binding than the wild type ( i.e. GalNAc-type glycopeptide). The crystal structures of PILRα complexed with these glycopeptides highlighted the importance of stereochemical positioning of the O4 atom of the sugar moiety. These results provide insights both for understanding the unique O -glycosylated peptide recognition by the PILRα and for the rational design of herpes simplex virus-1 entry inhibitors.


  • Organizational Affiliation

    From the Laboratories of Biomolecular Science and.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Paired immunoglobulin-like type 2 receptor alpha
A, B
120Homo sapiensMutation(s): 1 
Gene Names: PILRA
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UKJ1 (Homo sapiens)
Explore Q9UKJ1 
Go to UniProtKB:  Q9UKJ1
PHAROS:  Q9UKJ1
GTEx:  ENSG00000085514 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UKJ1
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Peptide from Envelope glycoprotein BC [auth X],
D [auth Y]
7Human alphaherpesvirus 1 strain KOSMutation(s): 0 
UniProt
Find proteins for P06437 (Human herpesvirus 1 (strain KOS))
Explore P06437 
Go to UniProtKB:  P06437
Entity Groups  
UniProt GroupP06437
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 3
MoleculeChains Length2D Diagram Glycosylation3D Interactions
N-acetyl-alpha-neuraminic acid-(2-6)-2-acetamido-2,4-dideoxy-alpha-D-xylo-hexopyranoseE [auth C],
F [auth D]
2N/A
Glycosylation Resources
GlyTouCan:  G15938JF
GlyCosmos:  G15938JF
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.229 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.28α = 90
b = 63.329β = 110.08
c = 55.072γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2017-10-25
    Type: Initial release
  • Version 1.1: 2018-01-24
    Changes: Database references
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Structure summary
  • Version 2.1: 2023-11-22
    Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary