Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0017194
Title: Understanding TR binding to pMHC complexes: How does a TR scan many pMHC complexes yet preferentially bind to one
Authors: Khan, J.M.
Ranganathan, S. 
Issue Date: 2011
Citation: Khan, J.M., Ranganathan, S. (2011). Understanding TR binding to pMHC complexes: How does a TR scan many pMHC complexes yet preferentially bind to one. PLoS ONE 6 (2) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0017194
Abstract: 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. © 2011 Khan, Ranganathan.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/108589
ISSN: 19326203
DOI: 10.1371/journal.pone.0017194
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