The coordination of unprotonated peptide tertiary structure as a metric of pMHC-TCR functional avidity

Georgios S E Antipas; Anastasios E Germenis

doi:10.1016/j.dib.2015.09.009

The coordination of unprotonated peptide tertiary structure as a metric of pMHC-TCR functional avidity

Data Brief. 2015 Sep 28:5:342-7. doi: 10.1016/j.dib.2015.09.009. eCollection 2015 Dec.

Authors

Georgios S E Antipas¹, Anastasios E Germenis²

Affiliations

¹ Division of Materials Technology, National Technical University of Athens, Zografou Campus, Athens 15780, Greece.
² Department of Immunology & Histocompatibility, School of Medicine, University of Thessaly, Biopolis, Larissa 41110, Greece.

Abstract

The coordination difference between the unprotonated tertiary structures of a native (Tax) peptide and a number of its variants - all peptides presented by HLA-A201 and bound to the human A6 T cell receptor-was discovered to constitute a metric of pMHC-TCR functional avidity. Moreover, increasing coordination deviations from the index were found to flag correspondingly weakening immunological outcomes of the variant peptides. The prognostic utility of the coordination difference of unprotonated tertiary structure was established to operate strictly on the peptide scale, seizing to be of relevance either to the immediate peptide environment (i.e. within the realm of peptide short range order, within 7 Å of any peptide atom) or over the entirety of the pMHC-TCR complex. Additionally, the imprint of peptide immunological identity was expressed both by the total coordination as well as by its C-C partial.

Keywords: Atomic pair correlation; Cumulative coordination; Functional avidity; Short range order; Structure–function relationship; pMHC–TCR interaction.