How peptide/MHC presence affects the dynamics of the LC13 T-cell receptor
| Autor: | Bernhard Knapp, José L. Domínguez |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Protein Conformation T-Lymphocytes Receptors Antigen T-Cell lcsh:Medicine chemical and pharmacologic phenomena Molecular Dynamics Simulation Major histocompatibility complex Article Accessible surface area Structure-Activity Relationship 03 medical and health sciences 0302 clinical medicine Protein structure Antigen HLA Antigens Histocompatibility Antigens Humans Binding site Antigen-presenting cell Receptor lcsh:Science Antigen Presentation Binding Sites Multidisciplinary biology Chemistry T-cell receptor lcsh:R Hydrogen Bonding hemic and immune systems Molecular Docking Simulation 030104 developmental biology biology.protein Biophysics lcsh:Q Peptides Algorithms 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Scientific Reports, Vol 9, Iss 1, Pp 1-11 (2019) Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | The interaction between T-cell receptors (TCRs) of T-cells and potentially immunogenic peptides presented by MHCs of antigen presenting cells is one of the most important mechanisms of the adaptive human immune system. A large number of structural simulations of the TCR/peptide/MHC system have been carried out. However, to date no study has investigated the differences of the dynamics between free TCRs and pMHC bound TCRs on a large scale. Here we present a study totalling 37 100 ns investigating the LC13 TCR in its free form as well as in complex with HLA-B*08:01 and different peptides. Our results show that the dynamics of the bound and unbound LC13 TCR differ significantly. This is reflected in (a) expected results such as an increased flexibility and increased solvent accessible surface of the CDRs of unbound TCR simulations but also in (b) less expected results such as lower CDR distances and compactness as well as alteration in the hydrogen bond network around CDR3α of unbound TCR simulations. Our study further emphasises the structural flexibility of TCRs and confirms the importance of the CDR3 loops for the adoption to MHC. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |