Pillars Article: The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
By Pamela J. Bjorkman, M. Saper, B. Samraoui, W. Bennett, J. Strominger, D. Wiley. Journal of Immunology, 2005
1,704 citations recorded by the source corpus.
Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/42ccd0e5a4cc91b10a926c614489d5f54dbf9774
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In Immunology
In Molecular Biology
- Alessandro Sette
- Bjoern Peters
- John Sidney
- K. Rock
- Morten Nielsen
- Massimo Andreatta
- Ole Lund
- Sinu Paul
Citations in the corpus
- Evolution of the immune system in humans from infancy to old age (2015, neutral): “Add to this considerable genetic variability in how individuals respond, determined by the highly polymorphic HLA genes [67] and by the genes of innate immunity, and it is not surprising that the immune responses of any single adult vary considerably.”
- HLA class I supertypes: a revised and updated classification (2008, background): “Typically, in the case of human leukocyte antigen (HLA) class I, the main binding energy is provided by the interaction of residues in position 2 and the C-terminus of the peptide with the B and F binding pockets of the MHC molecule, respectively [1-8], although side chains throughout the ligand can”
- Present Yourself! By MHC Class I and MHC Class II Molecules (2016, background): “This capital structure generated a peptide-binding groove between the alpha helixes[2, 3], which is ‘evolutionarily speaking’ likely borrowed from earlier chaperone structures.”