select ad.sno,ad.journal,ad.title,ad.author_names,ad.abstract,ad.abstractlink,j.j_name,vi.* from articles_data ad left join journals j on j.journal=ad.journal left join vol_issues vi on vi.issue_id_en=ad.issue_id where ad.sno_en='7939' and ad.lang_id='9' and j.lang_id='9' and vi.lang_id='9' Peptide length significantly influences in vitro affinity fo | 7939
రోగనిరోధక పరిశోధన

రోగనిరోధక పరిశోధన
అందరికి ప్రవేశం

ISSN: 1745-7580

నైరూప్య

Peptide length significantly influences in vitro affinity for MHC class II molecules

Cathal O'Brien, Darren R Flower

Background: Class II Major Histocompatibility Complex (MHC) molecules have an open-ended binding groove which can accommodate peptides of varying lengths. Several studies have demonstrated that peptide flanking residues (PFRs) which lie outside the core binding groove can influence peptide binding and T cell recognition. By using data from the AntiJen database we were able to characterise systematically the influence of PFRs on peptide affinity for MHC class II molecules. Results: By analysing 1279 peptide elongation events covering 19 distinct HLA alleles it was observed that, in general, peptide elongation resulted in increased MHC class II molecule affinity. It was also possible to determine an optimal peptide length for MHC class II affinity of approximately 18–20 amino acids; elongation of peptides beyond this length resulted in a null or negative effect on affinity. Conclusion: The observed relationship between peptide length and MHC class II affinity has significant implications for the design of vaccines and the study of the epitopic basis of immunological disease.

నిరాకరణ: ఈ సారాంశం కృత్రిమ మేధస్సు సాధనాలను ఉపయోగించి అనువదించబడింది మరియు ఇంకా సమీక్షించబడలేదు లేదా ధృవీకరించబడలేదు.
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