PMID- 23046123
OWN - NLM
STAT- MEDLINE
DCOM- 20130225
LR  - 20211021
IS  - 1600-065X (Electronic)
IS  - 0105-2896 (Linking)
VI  - 250
IP  - 1
DP  - 2012 Nov
TI  - A structural voyage toward an understanding of the MHC-I-restricted immune 
      response: lessons learned and much to be learned.
PG  - 61-81
LID - 10.1111/j.1600-065X.2012.01159.x [doi]
AB  - T cells that express clonally distributed alphabeta T-cell receptors (TCRs) corecognize 
      antigenic peptides (p) bound to major histocompatibility complex class I (MHC-I) 
      and class II molecules (MHC-II). Extensive human leukocyte antigen (HLA) 
      polymorphism enables HLA molecules from different haplotypes to capture an array 
      of self- and microbe-derived peptide antigens that is fundamental to adaptive 
      immunity. T cells developing in the thymus are selected for weak binding to 
      self-peptide-HLA complexes generating a vast repertoire of clonally distinct T 
      cells in the periphery. Indeed, diversity within germline loci and the finally 
      assembled TCR genes, coupled with inherent TCR cross-reactivity, enables CD8(+) T 
      cells to survey the multitude of pHLA-I landscapes. Precisely how does the TCR 
      ligate to pHLA-I, and how does knowledge of the detailed structural interactions 
      inform immunobiology? A recent number of our structural studies concerning the 
      TCR-pMHC-I axis, alongside others in the field, have provided insight into HLA-I 
      polymorphism, pMHC-I flexibility, TCR bias, TCR polymorphism, maintenance of 
      self-tolerance, T-cell cross-reactivity, and alloreactivity. Collectively, the 
      data also provide an opportunity to address the structural correlates of MHC-I 
      restriction. Here, we provide our perspective concerning these advances in the 
      field. Although much key information has been gleaned, the structural data show 
      that some of the key concepts surrounding the TCR-pMHC-I interaction remain 
      controversial and unresolved.
CI  - (c) 2012 John Wiley & Sons A/S.
FAU - Gras, Stephanie
AU  - Gras S
AD  - Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, 
      Monash University, Clayton, Australia.
FAU - Burrows, Scott R
AU  - Burrows SR
FAU - Turner, Stephen J
AU  - Turner SJ
FAU - Sewell, Andrew K
AU  - Sewell AK
FAU - McCluskey, James
AU  - McCluskey J
FAU - Rossjohn, Jamie
AU  - Rossjohn J
LA  - eng
GR  - BB/H001085/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Immunol Rev
JT  - Immunological reviews
JID - 7702118
RN  - 0 (HLA Antigens)
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Peptides)
RN  - 0 (Receptors, Antigen, T-Cell, alpha-beta)
SB  - IM
MH  - Adaptive Immunity
MH  - Animals
MH  - Binding Sites
MH  - Cross Reactions
MH  - HLA Antigens/*chemistry/immunology/metabolism
MH  - Histocompatibility Antigens Class I/*chemistry/immunology/metabolism
MH  - Humans
MH  - Major Histocompatibility Complex/*immunology
MH  - Mice
MH  - Models, Molecular
MH  - Peptides/*chemistry/immunology/metabolism
MH  - Protein Binding
MH  - Protein Conformation
MH  - Receptors, Antigen, T-Cell, alpha-beta/*chemistry/immunology/metabolism
MH  - T-Lymphocytes/cytology/*immunology/metabolism
EDAT- 2012/10/11 06:00
MHDA- 2013/02/26 06:00
CRDT- 2012/10/11 06:00
PHST- 2012/10/11 06:00 [entrez]
PHST- 2012/10/11 06:00 [pubmed]
PHST- 2013/02/26 06:00 [medline]
AID - 10.1111/j.1600-065X.2012.01159.x [doi]
PST - ppublish
SO  - Immunol Rev. 2012 Nov;250(1):61-81. doi: 10.1111/j.1600-065X.2012.01159.x.