Recognition of core and flanking amino acids of MHC class II-bound peptides by the T cell receptor Journal Article

  


Authors: Sant'angelo, D. B.; Robinson, E.; Janeway, C. A. Jr; Denzin, L. K.
Article Title: Recognition of core and flanking amino acids of MHC class II-bound peptides by the T cell receptor
Abstract: CD4 T cells recognize peptides bound to major histocompatibility complex (MHC) class II molecules. Most MHC class II molecules have four binding pockets occupied by amino acids 1, 4, 6, and 9 of the minimal peptide epitope, while the residues at positions 2, 3, 5, 7, and 8 are available to interact with the T cell receptor (TCR). In addition MHC class II bound peptides have flanking residues situated outside of this peptide core. Here we demonstrate that the flanking residues of the conalbumin peptide bound to I-Ak have no effect on recognition by the D10 TCR. To study the role of peptide flanks for recognition by a second TCR, we determined the MHC and TCR contacting amino acids of the I-Ab bound Eα peptide. The Eα peptide is shown to bind I-Ab using four alanines as anchor residues. TCR recognition of Eα peptides with altered flanking residues again suggested that, in general, no specific interactions occurred with the peptide flanks. However, using an HLA-DM-mediated technique to measure peptide binding to MHC class II molecules, we found that the peptide flanking residues contribute substantially to MHC binding.
Keywords: controlled study; core protein; nonhuman; t lymphocyte; animal cell; mouse; animals; mice; animal tissue; analytic method; protein binding; peptide; transfection; structure-activity relationship; mice, inbred c57bl; t lymphocyte receptor; antigen presentation; amino acid sequence; molecular sequence data; antigen; receptors, antigen, t-cell; sequence alignment; major histocompatibility antigen class 2; antigen recognition; peptide fragments; epitope; peptides; dna flanking region; binding sites; cd4 antigen; alanine; protein structure; antigen binding; histocompatibility antigens class ii; structure analysis; hla dm antigen; hla-d antigens; cell activity; receptor binding; ovotransferrin; chickens; peptide derivative; epitopes; mhc; tcr; t cell; consensus sequence; antigens, differentiation, b-lymphocyte; antibody combining site; amino acid derivative; humans; priority journal; article; conalbumin
Journal Title: European Journal of Immunology
Volume: 32
Issue: 9
ISSN: 0014-2980
Publisher: Wiley V C H Verlag Gmbh  
Date Published: 2002-09-01
Start Page: 2510
End Page: 2520
Language: English
DOI: 10.1002/1521-4141(200209)32:9<2510::aid-immu2510>3.0.co;2-q
PUBMED: 12207335
PROVIDER: scopus
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-0036740190&partnerID=40&md5=19a8b3fefff8809a09b762c6dcfbf082
Notes: Export Date: 14 November 2014 -- Source: Scopus
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MSK Authors
  1. Lisa K Denzin
    22 Denzin
  2. Derek B Sant'angelo
    46 Sant'angelo
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