Understanding TR binding to pMHC complexes

how does a TR scan many pMHC complexes yet preferentially bind to one

Javed Mohammed Khan, Shoba Ranganathan*

*Corresponding author for this work

Research output: Contribution to journalArticle

8 Citations (Scopus)
10 Downloads (Pure)


Understanding the basis of the binding of a T cell receptor (TR) to the peptide-MHC (pMHC) complex is essential due to the vital role it plays in adaptive immune response. We describe the use of computed binding (free) energy (BE), TR paratope, pMHC epitope, molecular surface electrostatic potential (MSEP) and calculated TR docking angle (θ) to analyse 61 TR/pMHC crystallographic structures to comprehend TR/pMHC interaction. In doing so, we have successfully demonstrated a novel/rational approach for θ calculation, obtained a linear correlation between BE and θ without any "codon" or amino acid preference, provided an explanation for TR ability to scan many pMHC ligands yet specifically bind one, proposed a mechanism for pMHC recognition by TR leading to T cell activation and illustrated the importance of the peptide in determining TR specificity, challenging the "germline bias" theory.

Original languageEnglish
Article numbere17194
Pages (from-to)1-12
Number of pages12
JournalPLoS ONE
Issue number2
Publication statusPublished - 2011

Bibliographical note

Copyright the Author(s) 2011. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

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