Major Histocompatibility Complex class I (MHC I) molecules are highly polymorphic, with allotypes differing in peptide binding preferences, and in their dependence upon tapasin for optimal peptide selection. The tapasin dependence of MHC allotypes is inversely correlated with their self-editing ability, and underpinned by conformational plasticity. Recently, TAPBPR has been shown to enhance MHC I assembly via a chaperone-like function, and by editing the peptide repertoire of some MHC I allotypes. Structural analysis has shown TAPBPR binding changes the conformation and dynamics of MHC I, with MHC protein dynamics likely to determine the prevailing TAPBPR function: generically enhancing MHC I assembly by stabilising highly dynamic peptide-empty MHC I; and by editing the peptide repertoire of highly dynamic MHC I allotypes.
Journal article
2021-06-01T00:00:00+00:00
70
138 - 143
5
Institute for Life Sciences and Centre for Cancer Immunology, Faculty of Medicine, University of Southampton, Building 85, Southampton, SO17 1BJ, UK.
Humans, Peptides, Immunoglobulins, Membrane Transport Proteins, Membrane Proteins, Histocompatibility Antigens Class I