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PDBsum entry 4qrr

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protein ligands Protein-protein interface(s) links
Immune system PDB id
4qrr

 

 

 

 

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Contents
Protein chains
276 a.a.
99 a.a.
203 a.a.
241 a.a.
Ligands
ILE-PRO-SER-ILE-
ASN-VAL-HIS-HIS-
TYR
Waters ×23
PDB id:
4qrr
Name: Immune system
Title: Crystal structure of hla b 3501-Ips in complex with a delta-beta tcr, clone 12 tcr
Structure: Hla class i histocompatibility antigen, b-35 alpha chain. Chain: a. Synonym: mhc class i antigen b 35. Engineered: yes. Beta-2-microglobulin. Chain: b. Synonym: beta-2-microglobulin form pi 5.3. Engineered: yes. Clone12 tcr beta chain.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-b, hlab. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: b2m, cdabp0092, hdcma22p. Synthetic: yes. Human herpesvirus 5.
Resolution:
3.00Å     R-factor:   0.213     R-free:   0.258
Authors: S.Gras,E.Chabrol,J.Rossjohn
Key ref: D.G.Pellicci et al. (2014). The molecular bases of δ/αβ T cell-mediated antigen recognition. J Exp Med, 211, 2599-2615. PubMed id: 25452463 DOI: 10.1084/jem.20141764
Date:
02-Jul-14     Release date:   10-Dec-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01889  (1B07_HUMAN) -  HLA class I histocompatibility antigen, B alpha chain from Homo sapiens
Seq:
Struc:
362 a.a.
276 a.a.*
Protein chain
Pfam   ArchSchema ?
P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens
Seq:
Struc:
119 a.a.
99 a.a.
Protein chain
No UniProt id for this chain
Struc: 203 a.a.
Protein chain
No UniProt id for this chain
Struc: 241 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 22 residue positions (black crosses)

 

 
DOI no: 10.1084/jem.20141764 J Exp Med 211:2599-2615 (2014)
PubMed id: 25452463  
 
 
The molecular bases of δ/αβ T cell-mediated antigen recognition.
D.G.Pellicci, A.P.Uldrich, J.Le Nours, F.Ross, E.Chabrol, S.B.Eckle, R.de Boer, R.T.Lim, K.McPherson, G.Besra, A.R.Howell, L.Moretta, J.McCluskey, M.H.Heemskerk, S.Gras, J.Rossjohn, D.I.Godfrey.
 
  ABSTRACT  
 
αβ and γδ T cells are disparate T cell lineages that can respond to distinct antigens (Ags) via the use of the αβ and γδ T cell Ag receptors (TCRs), respectively. Here we characterize a population of human T cells, which we term δ/αβ T cells, expressing TCRs comprised of a TCR-δ variable gene (Vδ1) fused to joining α and constant α domains, paired with an array of TCR-β chains. We demonstrate that these cells, which represent ∼50% of all Vδ1(+) human T cells, can recognize peptide- and lipid-based Ags presented by human leukocyte antigen (HLA) and CD1d, respectively. Similar to type I natural killer T (NKT) cells, CD1d-lipid Ag-reactive δ/αβ T cells recognized α-galactosylceramide (α-GalCer); however, their fine specificity for other lipid Ags presented by CD1d, such as α-glucosylceramide, was distinct from type I NKT cells. Thus, δ/αβTCRs contribute new patterns of Ag specificity to the human immune system. Furthermore, we provide the molecular bases of how δ/αβTCRs bind to their targets, with the Vδ1-encoded region providing a major contribution to δ/αβTCR binding. Our findings highlight how components from αβ and γδTCR gene loci can recombine to confer Ag specificity, thus expanding our understanding of T cell biology and TCR diversity.
 

 

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