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Thermodynamics Of Peptide-Mhc Class Ii Interactions: Not All Complexes Are Created Equal
|Title||Thermodynamics Of Peptide-Mhc Class Ii Interactions: Not All Complexes Are Created Equal|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Journal||Frontiers in Immunology|
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.