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Structure of Human T-complex protein 1 subunit epsilon (CCT5)
Structural highlights
DiseaseTCPE_HUMAN Hereditary sensory and autonomic neuropathy with spastic paraplegia. The disease is caused by mutations affecting the gene represented in this entry. FunctionTCPE_HUMAN Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.[1] Publication Abstract from PubMedThe human chaperonin TRiC consists of eight non-identical subunits, and its protein-folding activity is critical for cellular health. Misfolded proteins are associated with many human diseases, such as amyloid diseases, cancer, and neuropathies, making TRiC a potential therapeutic target. A detailed structural understanding of its ATP-dependent folding mechanism and substrate recognition is therefore of great importance. Of particular health-related interest is the mutation Histidine 147 to Arginine (H147R) in human TRiC subunit 5 (CCT5), which has been associated with hereditary sensory neuropathy. In this paper, we describe the crystal structures of CCT5 and the CCT5-H147R mutant, which provide important structural information for this vital protein-folding machine in humans. This first X-ray crystallographic study of a single human CCT subunit in the context of a hexadecameric complex can be expanded in the future to the other 7 subunits that form the TRiC complex. Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.,Pereira JH, McAndrew RP, Sergeeva OA, Ralston CY, King JA, Adams PD Sci Rep. 2017 Jun 16;7(1):3673. doi: 10.1038/s41598-017-03825-3. PMID:28623285[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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