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

O'Brien, Cathal, Flower, Darren R and Feighery, Conleth (2008). Peptide length significantly influences in vitro affinity for MHC class II molecules. Immunome Research, 4 (6),

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.

Publication DOI: https://doi.org/10.1186/1745-7580-4-6
Divisions: Life & Health Sciences > Pharmacy
Life & Health Sciences
Additional Information: © 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.
Uncontrolled Keywords: Immunology,Molecular Biology,Computational Theory and Mathematics,Applied Mathematics,Computer Science Applications
Full Text Link: http://www.immu ... m/content/4/1/6
Related URLs: http://www.scop ... tnerID=8YFLogxK (Scopus URL)
Published Date: 2008-11-26
Authors: O'Brien, Cathal
Flower, Darren R ( 0000-0002-8542-7067)
Feighery, Conleth

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License: Creative Commons Attribution


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