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Binding immunoglobulin protein
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Binding immunoglobulin protein (BiP) (also called glucose regulated protein 78, Grp78) is a molecular chaperone that uses ATP/ADP cycling to regulate protein folding by the Protein Disulfide Isomerase (PDI) family of proteins. It is a 78kDa glucose-regulated heat shock protein and is involved in unfolded protein response. HSPA5 is its human gene. It binds to immunoglobulin heavy chain.
the nucleotide-binding domain of GRP78 interacts with ATP, its substrate-binding domain can interact with unfolded/misfolded protein.

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Encyclopedia
Binding immunoglobulin protein (BiP) (also called glucose regulated protein 78, Grp78) is a molecular chaperone that uses ATP/ADP cycling to regulate protein folding by the Protein Disulfide Isomerase (PDI) family of proteins. It is a 78kDa glucose-regulated heat shock protein and is involved in unfolded protein response. HSPA5 is its human gene. It binds to immunoglobulin heavy chain.
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 PDI can then work to promote disulfide oxidation and rearrangement 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.
Further reading
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