Peptide cargo tunes a network of correlated motions in human leucocyte antigens.

ABSTRACT: Most biomolecular interactions are typically thought to increase the (local) rigidity of a complex, for example, in drug-target binding. However, detailed analysis of specific biomolecular complexes can reveal a more subtle interplay between binding and rigidity. Here, we focussed on the human leucocyte antigen (HLA), which plays a crucial role in the adaptive immune system by presenting peptides for recognition by the αβ T-cell receptor (TCR). The role that the peptide plays in tuning HLA flexibility during TCR recognition is potentially crucial in determining the functional outcome of an immune response, with obvious relevance to the growing list of immunotherapies that target the T-cell compartment. We have applied high-pressure/temperature perturbation experiments, combined with molecu

SUBMITTER: Hopkins JR 

PROVIDER: S-EPMC8651013 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature