Binding immunoglobulin protein

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 (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 BiP interacts with ATP, its substrate-binding domain can interact with unfolded/misfolded protein. Subsequent ATP hydrolysis acts to strengthen the interaction between BiP 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 BiP 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 BiP binding.

PBB_Summary
section_title =
summary_text = When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell. [supplied by OMIM] [cite web | title = Entrez Gene: HSPA5 heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3309| accessdate = ]

References

* [http://www.jbc.org/cgi/reprint/M002655200v1.pdf BiP and PDI cooperate in the oxidative folding of antibodies in vitro]

Further reading

PBB_Further_reading
citations =
*cite journal | author=Li J, Lee AS |title=Stress induction of GRP78/BiP and its role in cancer. |journal=Curr. Mol. Med. |volume=6 |issue= 1 |pages= 45–54 |year= 2006 |pmid= 16472112 |doi=

External links

*

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