6U3N

LS2.8/3.15 - DQ2-P.fluor-alpha1a complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

T cell receptor cross-reactivity between gliadin and bacterial peptides in celiac disease.

Petersen, J.Ciacchi, L.Tran, M.T.Loh, K.L.Kooy-Winkelaar, Y.Croft, N.P.Hardy, M.Y.Chen, Z.McCluskey, J.Anderson, R.P.Purcell, A.W.Tye-Din, J.A.Koning, F.Reid, H.H.Rossjohn, J.

(2020) Nat Struct Mol Biol 27: 49-61

  • DOI: https://doi.org/10.1038/s41594-019-0353-4
  • Primary Citation of Related Structures:  
    6U3M, 6U3N, 6U3O

  • PubMed Abstract: 

    The human leukocyte antigen (HLA) locus is strongly associated with T cell-mediated autoimmune disorders. HLA-DQ2.5-mediated celiac disease (CeD) is triggered by the ingestion of gluten, although the relative roles of genetic and environmental risk factors in CeD is unclear. Here we identify microbially derived mimics of gliadin epitopes and a parental bacterial protein that is naturally processed by antigen-presenting cells and activated gliadin reactive HLA-DQ2.5-restricted T cells derived from CeD patients. Crystal structures of T cell receptors in complex with HLA-DQ2.5 bound to two distinct bacterial peptides demonstrate that molecular mimicry underpins cross-reactivity toward the gliadin epitopes. Accordingly, gliadin reactive T cells involved in CeD pathogenesis cross-react with ubiquitous bacterial peptides, thereby suggesting microbial exposure as a potential environmental factor in CeD.


  • Organizational Affiliation

    Infection and Immunity Program and The Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute Monash University, Clayton, Victoria, Australia.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
T-CELL RECEPTOR, LS2.8/3.15 alphaA [auth D]206Homo sapiensMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
T-CELL RECEPTOR, LS2.8/3.15 betaB [auth E]244Homo sapiensMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
MHC class II HLA-DQ-alpha chainC [auth A]191Homo sapiensMutation(s): 0 
Gene Names: HLA-DQA1
UniProt & NIH Common Fund Data Resources
Find proteins for P01909 (Homo sapiens)
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Go to UniProtKB:  P01909
PHAROS:  P01909
GTEx:  ENSG00000196735 
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UniProt GroupP01909
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
MHC class II HLA-DQ-beta-1D [auth B]206Homo sapiensMutation(s): 0 
Gene Names: HLA-DQB1
UniProt
Find proteins for O19712 (Homo sapiens)
Explore O19712 
Go to UniProtKB:  O19712
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UniProt GroupO19712
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
PeptideE [auth C]20Pseudomonas fluorescensMutation(s): 0 
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Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NAG
Query on NAG

Download Ideal Coordinates CCD File 
F [auth A]2-acetamido-2-deoxy-beta-D-glucopyranose
C8 H15 N O6
OVRNDRQMDRJTHS-FMDGEEDCSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.98α = 90
b = 239.47β = 90
c = 147.46γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Australian Research Council (ARC)AustraliaCE140100011

Revision History  (Full details and data files)

  • Version 1.0: 2019-12-18
    Type: Initial release
  • Version 1.1: 2020-07-01
    Changes: Data collection, Database references
  • Version 1.2: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Derived calculations, Structure summary