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2000
Volume 14, Issue 6
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Major Histocompatibility Complex (MHC) molecules are cell surface glycoproteins that are central to the process of immunity. MHC Class I and II molecules differ in their peptide binding specificity. In this study we have analyzed a non redundant set of MHC binding peptides derived from MHCPEP database, in terms of tripeptides and their positional preference. Results indicate that certain tripeptides have a preference to appear at a particular position for a specific allele. Further, the distribution of rigid tripeptides across all binding sequences was also analyzed and their positions were correlated with anchor residue positions.

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/content/journals/ppl/10.2174/092986607780989895
2007-06-01
2025-05-20
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/content/journals/ppl/10.2174/092986607780989895
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  • Article Type:
    Research Article
Keyword(s): MHC peptides; MHCPEP; Nonamers; Positional preference; Rigid tripeptides; Tripeptides
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