Antipas Georgios S E, Germenis Anastasios E
Division of Materials Technology, National Technical University of Athens, Zografou Campus, Athens 15780, Greece.
Department of Immunology & Histocompatibility, School of Medicine, University of Thessaly, Biopolis, Larissa 41110, Greece.
Data Brief. 2015 Sep 28;5:342-7. doi: 10.1016/j.dib.2015.09.009. eCollection 2015 Dec.
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.
研究发现，天然（Tax）肽及其多种变体的未质子化三级结构之间的配位差异——所有这些肽均由HLA - A201呈递并与人A6 T细胞受体结合——构成了pMHC - TCR功能亲和力的一个衡量指标。此外，发现与该指标的配位偏差增加相应地表明变体肽的免疫结果减弱。未质子化三级结构的配位差异的预后效用被确定严格在肽尺度上起作用，在紧邻肽的环境（即肽短程有序范围内，任何肽原子7 Å以内）或整个pMHC - TCR复合物范围内均不再具有相关性。此外，肽免疫特性的印记通过总配位及其C - C部分配位来体现。
