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

Cathal O'Brien, Darren R Flower, Conleth Feighery

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish
Article number6
Number of pages7
JournalImmunome Research
Volume4
Issue number6
DOIs
Publication statusPublished - 26 Nov 2008

Bibliographical note

© 2008 O'Brien et al; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Fingerprint

Dive into the research topics of 'Peptide length significantly influences in vitro affinity for MHC class II molecules'. Together they form a unique fingerprint.

Cite this