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PDBsum entry 3mv8

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protein ligands Protein-protein interface(s) links
Immune system PDB id
3mv8

 

 

 

 

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Contents
Protein chains
276 a.a. *
100 a.a. *
11 a.a. *
200 a.a. *
242 a.a. *
Ligands
SO4
Waters ×201
* Residue conservation analysis
PDB id:
3mv8
Name: Immune system
Title: Crystal structure of the tk3-gln55his tcr in complex with hla- b 3501/Hpvg
Structure: Hla class i histocompatibility antigen, b-35 alpha chain. Chain: a. Fragment: extracellular domain. Synonym: hla b 3501 Heavy chain, mhc class i antigen b 35. Engineered: yes. Beta-2-microglobulin. Chain: b. Synonym: beta-2-microglobulin form pi 5.3. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-b, hlab. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: b2m, cdabp0092, hdcma22p. Synthetic: yes. Other_details: synthetic peptide.
Resolution:
2.10Å     R-factor:   0.231     R-free:   0.276
Authors: S.Gras,Z.Chen,J.J.Miles,Y.C.Liu,M.J.Bell,L.C.Sullivan,L.Kjer-Nielsen, R.M.Brennan,J.M.Burrows,M.A.Neller,R.Khanna,A.W.Purcell,A.G.Brooks, J.Mccluskey,J.Rossjohn,S.R.Burrows
Key ref: S.Gras et al. (2010). Allelic polymorphism in the T cell receptor and its impact on immune responses. J Exp Med, 207, 1555-1567. PubMed id: 20566715
Date:
03-May-10     Release date:   09-Jun-10    
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.
100 a.a.*
Protein chain
Pfam   ArchSchema ?
P03211  (EBNA1_EBVB9) -  Epstein-Barr nuclear antigen 1 from Epstein-Barr virus (strain B95-8)
Seq:
Struc:
 
Seq:
Struc:
641 a.a.
11 a.a.
Protein chain
No UniProt id for this chain
Struc: 200 a.a.
Protein chain
No UniProt id for this chain
Struc: 242 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 23 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain C: E.C.3.1.21.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Exp Med 207:1555-1567 (2010)
PubMed id: 20566715  
 
 
Allelic polymorphism in the T cell receptor and its impact on immune responses.
S.Gras, Z.Chen, J.J.Miles, Y.C.Liu, M.J.Bell, L.C.Sullivan, L.Kjer-Nielsen, R.M.Brennan, J.M.Burrows, M.A.Neller, R.Khanna, A.W.Purcell, A.G.Brooks, J.McCluskey, J.Rossjohn, S.R.Burrows.
 
  ABSTRACT  
 
In comparison to human leukocyte antigen (HLA) polymorphism, the impact of allelic sequence variation within T cell receptor (TCR) loci is much less understood. Particular TCR loci have been associated with autoimmunity, but the molecular basis for this phenomenon is undefined. We examined the T cell response to an HLA-B*3501-restricted epitope (HPVGEADYFEY) from Epstein-Barr virus (EBV), which is frequently dominated by a TRBV9*01(+) public TCR (TK3). However, the common allelic variant TRBV9*02, which differs by a single amino acid near the CDR2beta loop (Gln55-->His55), was never used in this response. The structure of the TK3 TCR, its allelic variant, and a nonnaturally occurring mutant (Gln55-->Ala55) in complex with HLA-B*3501(HPVGEADYFEY) revealed that the Gln55-->His55 polymorphism affected the charge complementarity at the TCR-peptide-MHC interface, resulting in reduced functional recognition of the cognate and naturally occurring variants of this EBV peptide. Thus, polymorphism in the TCR loci may contribute toward variability in immune responses and the outcome of infection.
 

 

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