Understanding TR binding to pMHC complexes: how does a TR scan many pMHC complexes yet preferentially bind to one.
Where this comes from
- Record sourced from PubMed, PMID 21364947.
- Also identified by DOI 10.1371/journal.pone.0017194 and PMC identifier 3043089.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Histocompatibility Antigens Class I
- Receptors, Antigen, T-Cell
- T-Cell Antigen Receptor Specificity