TRiC (complex)
T-complex protein Ring Complex, otherwise known as Chaperonin Containing TCP-1, is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates. TRiC is an example of a Biological machines that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis.
Subunits
The human TRiC complex is formed by two rings containing 8 similar but non-identical subunits, each with molecular weights of ~60 kDa. The two rings are stacked in an asymmetrical fashion, forming a barrel-like structure with a molecular weight of ~1 MDa.| Subunit | MW | Features |
| TCP1 | 60 | |
| CCT2 | 57 | |
| CCT3 | 61 | |
| CCT4 | 58 | |
| CCT5 | 60 | |
| CCT6 | 58 | Two copies in human genome, CCT6A and CCT6B. |
| CCT7 | 59 | |
| CCT8 | 60 |
Molecular weight of human subunits.