All Topics  
Binding immunoglobulin protein

 

   Email Print
   Bookmark   Link






 

Binding immunoglobulin protein



 
 
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
Protein disulfide isomerase

Protein disulfide isomerase or PDI is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold....
 (PDI) family of proteins. It is a 78kDa glucose-regulated heat shock protein
Heat shock protein

Heat shock proteins are a class of functionally related proteins whose expression is increased when cell are exposed to elevated temperatures or other stress....
 and is involved in unfolded protein response
Unfolded protein response

The unfolded protein response is a cellular stress response related to the endoplasmic reticulum. It is a stress response that has been found to be conserved between all mammalian species, as well as yeast and worm organisms....
. HSPA5 is its human gene
Gene

A gene is the basic unit of heredity in a living organism. All living things depend on genes. Genes hold the information to build and maintain their cell and pass genetic trait to offspring....
. 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.






Discussion
Ask a question about 'Binding immunoglobulin protein'
Start a new discussion about 'Binding immunoglobulin protein'
Answer questions from other users
Full Discussion Forum



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
Protein disulfide isomerase

Protein disulfide isomerase or PDI is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold....
 (PDI) family of proteins. It is a 78kDa glucose-regulated heat shock protein
Heat shock protein

Heat shock proteins are a class of functionally related proteins whose expression is increased when cell are exposed to elevated temperatures or other stress....
 and is involved in unfolded protein response
Unfolded protein response

The unfolded protein response is a cellular stress response related to the endoplasmic reticulum. It is a stress response that has been found to be conserved between all mammalian species, as well as yeast and worm organisms....
. HSPA5 is its human gene
Gene

A gene is the basic unit of heredity in a living organism. All living things depend on genes. Genes hold the information to build and maintain their cell and pass genetic trait to offspring....
. 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


External links