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.
Keywords: Tripeptides, MHC peptides, Rigid tripeptides, Positional preference, Nonamers, MHCPEP
Protein & Peptide Letters
Title: Distribution of Tripeptides in MHC Binding Peptides
Volume: 14 Issue: 6
Author(s): Sharmila Anishetty and Gautam Pennathur
Affiliation:
Keywords: Tripeptides, MHC peptides, Rigid tripeptides, Positional preference, Nonamers, MHCPEP
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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Cite this article as:
Sharmila Anishetty and Gautam Pennathur , Distribution of Tripeptides in MHC Binding Peptides, Protein & Peptide Letters 2007; 14 (6) . https://dx.doi.org/10.2174/092986607780989895
DOI https://dx.doi.org/10.2174/092986607780989895 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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