Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy
Author(s)Pereira, Jose H.; McAndrew, Ryan P.; Ralston, Corie Y.; King, Jonathan A.; Adams, Paul D.; Sergeeva, Oksana Andrei; ... Show more Show less
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The 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.
DepartmentMassachusetts Institute of Technology. Department of Biology
Nature Publishing Group
Pereira, Jose H. et al. “Structure of the Human TRiC/CCT Subunit 5 Associated with Hereditary Sensory Neuropathy.” Scientific Reports 7, 1 (June 2017): 3673 © 2017 The Author(s)
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