Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.

ABSTRACT: The MHC class I peptide loading complex (PLC) facilitates the assembly of MHC class I molecules with peptides, but factors that regulate the stability and dynamics of the assembly complex are largely uncharacterized. Based on initial findings that ATP, in addition to MHC class I-specific peptide, is able to induce MHC class I dissociation from the PLC, we investigated the interaction of ATP with the chaperone calreticulin, an endoplasmic reticulum (ER) luminal, calcium-binding component of the PLC that is known to bind ATP. We combined computational and experimental measurements to identify residues within the globular domain of calreticulin, in proximity to the high-affinity calcium-binding site, that are important for high-affinity ATP binding and for ATPase activity. High-affinity calci

SUBMITTER: Wijeyesakere SJ 

PROVIDER: S-EPMC4611598 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature