Application | Comment | Organism |
---|---|---|
drug development | development of small-molecule inhibitors of TRiC as potential antiviral therapeutics | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Homo sapiens | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain microvascular endothelial cell | HBMEC | Homo sapiens | - |
Caco-2 cell | - |
Homo sapiens | - |
HEK-293T cell | - |
Homo sapiens | - |
U2-OS cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Homo sapiens | ADP + phosphate | - |
? | |
additional information | reovirus sigma3 is a TRiC substrate | Homo sapiens | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
CCT | - |
Homo sapiens |
eukaryotic chaperonin TRiC | - |
Homo sapiens |
TRiC chaperonin | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | RNAi knockdown of each TRiC subunit substantially reduces the levels of intracellular reovirus proteins, providing evidence that TRiC is required for the production or stabilization of viral polypeptides | Homo sapiens |
additional information | TRiC redistributes to sites of viral replication. The TRiC chaperonin forms a complex with the reovirus sigma3 outer-capsid protein through an ATP-dependent mechanism | Homo sapiens |
physiological function | the eukaryotic TRiC chaperonin controls reovirus replication through outer-capsid folding, TRiC (also called CCT) is a cellular factor required for late events in the replication of mammalian reovirus. TRiC is essential for reovirus replication. TRiC forms a complex with the reovirus sigma3 outer-capsid protein and folds sigma3 into its into a native, assembly-competent conformation. TRiC renders sigma3 into a conformation that can assemble onto mature particles, which is a critical step in viral assembly, determination of a dynamic pathway for the efficient folding of viral capsid components mediated by the TRiC chaperonin, overview. Six of the eight subunits of the TRiC chaperonin (CCT1, CCT2, CCT3, CCT4, CCT5, and CCT8) are implicated in viral replication, siRNA mutational analysis, overview | Homo sapiens |