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PDBsum entry 3gsv

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Immune system PDB id
3gsv
Jmol
Contents
Protein chains
275 a.a. *
100 a.a. *
Ligands
ASN-LEU-VAL-PRO-
GLN-VAL-ALA-THR-
VAL
Waters ×150
* Residue conservation analysis
PDB id:
3gsv
Name: Immune system
Title: Crystal structure of the binary complex between hla-a2 and hcmv nlv-m5q peptide variant
Structure: Hla class i histocompatibility antigen, a-2 alpha chain. Chain: a. Synonym: mhc class i antigen a 2. Engineered: yes. Mutation: yes. Beta-2-microglobulin. Chain: b. Synonym: beta-2-microglobulin form pi 5.3.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla, hla-a, hlaa. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: b2m, beta-2 microglubulin, cdabp0092, hdcma22p. Synthetic: yes
Resolution:
1.90Å     R-factor:   0.206     R-free:   0.242
Authors: J.-B.Reiser,X.Saulquin,S.Gras,E.Debeaupuis,K.Echasserieau, A.Kissenpfennig,F.Legoux,A.Chouquet,M.Le Gorrec, P.Machillot,B.Neveu,N.Thielens,B.Malissen,M.Bonneville, D.Housset
Key ref: S.Gras et al. (2009). Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope. J Immunol, 183, 430-437. PubMed id: 19542454 DOI: 10.4049/jimmunol.0900556
Date:
27-Mar-09     Release date:   04-Aug-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01892  (1A02_HUMAN) -  HLA class I histocompatibility antigen, A-2 alpha chain
Seq:
Struc:
365 a.a.
275 a.a.*
Protein chain
Pfam   ArchSchema ?
P61769  (B2MG_HUMAN) -  Beta-2-microglobulin
Seq:
Struc:
119 a.a.
100 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   15 terms 
  Biological process     immune system process   21 terms 
  Biochemical function     protein binding     3 terms  

 

 
DOI no: 10.4049/jimmunol.0900556 J Immunol 183:430-437 (2009)
PubMed id: 19542454  
 
 
Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope.
S.Gras, X.Saulquin, J.B.Reiser, E.Debeaupuis, K.Echasserieau, A.Kissenpfennig, F.Legoux, A.Chouquet, M.Le Gorrec, P.Machillot, B.Neveu, N.Thielens, B.Malissen, M.Bonneville, D.Housset.
 
  ABSTRACT  
 
Protective T cell responses elicited along chronic human CMV (HCMV) infections are sometimes dominated by CD8 T cell clones bearing highly related or identical public TCR in unrelated individuals. To understand the principles that guide emergence of these public T cell responses, we have performed structural, biophysical, and functional analyses of an immunodominant public TCR (RA14) directed against a major HLA-A*0201-restricted HCMV Ag (pp65(495-503)) and selected in vivo from a diverse repertoire after chronic stimulations. Unlike the two immunodominant public TCRs crystallized so far, which focused on one peptide hotspot, the HCMV-specific RA14 TCR interacts with the full array of available peptide residues. The conservation of some peptide-MHC complex-contacting amino acids by lower-affinity TCRs suggests a shared TCR-peptide-MHC complex docking mode and supports an Ag-driven selection of optimal TCRs. Therefore, the emergence of a public TCR of an oligoclonal Ag-specific response after repeated viral stimulations is based on a receptor displaying a high structural complementarity with the entire peptide and focusing on three peptide hotspots. This highlights key parameters underlying the selection of a protective T cell response against HCMV infection, which remains a major health issue in patients undergoing bone marrow transplantation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23051753 L.Kjer-Nielsen, O.Patel, A.J.Corbett, J.Le Nours, B.Meehan, L.Liu, M.Bhati, Z.Chen, L.Kostenko, R.Reantragoon, N.A.Williamson, A.W.Purcell, N.L.Dudek, M.J.McConville, R.A.O'Hair, G.N.Khairallah, D.I.Godfrey, D.P.Fairlie, J.Rossjohn, and J.McCluskey (2012).
MR1 presents microbial vitamin B metabolites to MAIT cells.
  Nature, 491, 717-723.
PDB code: 4gup
  21301479 J.J.Miles, D.C.Douek, and D.A.Price (2011).
Bias in the αβ T-cell repertoire: implications for disease pathogenesis and vaccination.
  Immunol Cell Biol, 89, 375-387.  
21124993 J.J.Miles, A.M.Bulek, D.K.Cole, E.Gostick, A.J.Schauenburg, G.Dolton, V.Venturi, M.P.Davenport, M.P.Tan, S.R.Burrows, L.Wooldridge, D.A.Price, P.J.Rizkallah, and A.K.Sewell (2010).
Genetic and structural basis for selection of a ubiquitous T cell receptor deployed in Epstein-Barr virus infection.
  PLoS Pathog, 6, e1001198.
PDB code: 3o4l
20139278 L.Dong, P.Li, T.Oenema, C.L.McClurkan, and D.M.Koelle (2010).
Public TCR use by herpes simplex virus-2-specific human CD8 CTLs.
  J Immunol, 184, 3063-3071.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.