Anishettt Sharmila, Pennathur Gautam
Centre for Biotechnology, Anna University, Chennai-600025, India.
Protein Pept Lett. 2007;14(6):552-6. doi: 10.2174/092986607780989895.
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.
主要组织相容性复合体（MHC）分子是细胞表面糖蛋白，在免疫过程中起核心作用。MHC I类和II类分子在肽结合特异性方面存在差异。在本研究中，我们根据三肽及其位置偏好，分析了从MHCPEP数据库中获得的一组非冗余MHC结合肽。结果表明，某些三肽在特定等位基因的特定位置出现具有偏好性。此外，还分析了所有结合序列中刚性三肽的分布，并将它们的位置与锚定残基位置相关联。
