HSPD1

Description

The HSPD1 (heat shock protein family D (Hsp60) member 1) is a protein-coding gene located on chromosome 2.

HSPD1 (Heat shock protein family D member 1) is a mitochondrial chaperonin, essential for the proper folding of proteins. It is structurally and functionally similar to the bacterial GroEL protein. HSPD1 is involved in mitochondrial protein import, assisting in the folding of proteins transported from the cytoplasm into the mitochondrial matrix. It also plays a role in preventing misfolding and promoting the refolding of proteins under stress conditions. HSPD1 interacts with various proteins, including HRAS, HBV protein X, and HTLV-1 protein p40tax.

HSPD1, also known as Hsp60, is a chaperonin that plays a crucial role in mitochondrial protein import and macromolecular assembly. In collaboration with Hsp10, it assists in the proper folding of imported proteins. HSPD1 can also prevent misfolding and promote the refolding and proper assembly of unfolded proteins generated under stress conditions within the mitochondrial matrix. The functional unit of HSPD1 is a heptameric ring that forms a back-to-back double ring structure. This ring binds to an unfolded protein, followed by the binding of ATP and association with two heptameric rings of the co-chaperonin Hsp10. The unfolded protein is then sequestered within the inner cavity of HSPD1, allowing it to fold undisturbed. Synchronous hydrolysis of ATP within the HSPD1 subunits leads to the dissociation of the chaperonin rings, releasing ADP and the folded protein.

HSPD1 is also known as CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13.

Associated Diseases

• Autosomal dominant spastic paraplegia type 13
• Spastic paraplegia 13, autosomal dominant
• Leukodystrophy, hypomyelinating, 4