Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy

Pereira, Jose H.; McAndrew, Ryan P.; Sergeeva, Oksana A.; Ralston, Corie Y.; King, Jonathan A.; Adams, Paul D.

doi:10.1038/s41598-017-03825-3

Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy

Journal Article · Fri Jun 16 00:00:00 EDT 2017 · Scientific Reports

DOI:https://doi.org/10.1038/s41598-017-03825-3· OSTI ID:1379932

Pereira, Jose H. ^[1]; McAndrew, Ryan P. ^[1]; Sergeeva, Oksana A. ^[2]; Ralston, Corie Y. ^[3]; King, Jonathan A. ^[2]; Adams, Paul D. ^[4]

Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrated Bioimaging Division
Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States). Biology Dept.
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrated Bioimaging Division, Berkeley Center for Structural Biology
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrated Bioimaging Division; Univ. of California, Berkeley, CA (United States). Dept. of Bioengineering

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.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1379932

Journal Information:: Scientific Reports, Journal Name: Scientific Reports Journal Issue: 1 Vol. 7; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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