Mechanism
When the nucleotide-binding domain of GRP78 interacts with ATP, its substrate-binding domain can interact with unfolded/misfolded protein. Subsequent ATP hydrolysis acts to strengthen the interaction between GRP78 and the unfolded/misfolded protein. Under these conditions, protein disulfide isomerase (PDI) can then work to promote disulfide reduction, rearrangement, and reoxidation until the correct protein conformation is achieved. ADP/ATP exchange ends the interaction of GRP78 with the protein and thus PDI's work is halted, as well.
Once the correct protein structure is achieved, it is no longer a candidate for GRP78 binding.
Read more about this topic: Binding Immunoglobulin Protein
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