Anti-Chaperonin

HSPD1 (heat shock 60 kDa protein 1 (chaperonin)) is a member of the chaperonin family of proteins. Chaperonin may function as a signaling molecule in the innate immune system and is essential for the folding and assembly of newly imported proteins in the mitochondria implicated in mitochondrial protein import and macromolecular assembly. Diseases associated with HSPD1 include spastic paraplegia 13. It exists in two isoforms comprised of 573 amino acids. Chaperonin is expressed in adipose tissue, adrenal cortex, adrenal gland, blood and brain. Protein function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). [The UniProt Consortium]