Abstract
Recent advances suggest that the αβT-cell receptor bound to an antigenic peptide loaded major histocompatibility complex (pMHC) acts as a mechanosensor exhibiting “catch bond” behavior, which results in the lifetime of TCRαβ-pMHC association increasing upon application of physiological force. While catch bonds have been experimentally observed in TCRαβ-pMHC systems, the effects of load on conformational behavior remain unclear. Using molecular dynamics (MD) simulation, we recently proposed a model where the catch bond arises from allosteric pathways controlling TCRαβ subdomain motion through applied load.
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