thermodynamics of peptide-mhc class ii interactions: not all complexes are created equal
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2013
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Abstract
The adaptive immune response begins when CD4+ T cells recognize antigenic peptides bound to class II molecules of the Major Histocompatibility Complex (MHCII). The interaction between peptides and MHCII has been historically interpreted as a rigid docking event. However, this model has been challenged by the evidence that conformational flexibility plays an important role in peptide-MHCII complex formation. Thermodynamic analysis of the binding reaction suggests a model of complexation in which the physical-chemical nature of the peptide determines the variability in flexibility of the substates in the peptide-MHC conformational ensemble. This review discusses our understanding of the correlation between thermodynamics of peptide binding and structural features of the resulting complex as well as their impact on HLA-DM activity and on our ability to predict MHCII-restricted epitopes.
| Reference Key |
eferrante2013frontiersthermodynamics
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|---|---|
| Authors | ;Andrea eFerrante |
| Journal | sudebno-meditsinskaia ekspertiza |
| Year | 2013 |
| DOI |
10.3389/fimmu.2013.00308
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