EC Number   |
Cofactor |
Reference |
|---|
   3.6.4.B10 | more |
the group II CPNs do not require a GroES-like co-CPN but have a built-in lid that is composed of a helical protrusion in the apical domain. The rate of transfer of a substrate protein from PFD to CPN correlates with the strength of the PFD-CPN interaction |
757429 |
| 3.6.4.B10 | phosducin I |
- |
749858 |
| 3.6.4.B10 | phosducin II |
- |
749858 |
| 3.6.4.B10 | phosducin III |
- |
749858 |
| 3.6.4.B10 | phosducin-like cofactor protein |
three different phosducin-like cofactor proteins |
749858 |
| 3.6.4.B10 | prefoldin |
PFD, is a jellyfish-like hexameric protein that is exclusively found in archaea and eukaryotes, ans is a molecular chaperone that captures an unfolded protein substrate and transfers it to a group II chaperonin (CPN). The transfer of a substrate from PFD to CPN involves a direct interaction, PFD interacts with the apical domain of CPN. Analysis of protein-folding mechanism of PFD and CPN using the PFD-CPN systems of the hyperthermophilic archaea, the C-terminal region contributes to the functional cooperation between PFDalpha1beta1 and CPNbeta, overview. The C-terminus of the PFD alpha subunit is not important for the interaction with CPN and substrate transfer |
757429 |
| 3.6.4.B10 | prefoldin |
PFD, is required for protein substrate folding, PFD pivots around a conserved electrostatic interface with TRiC/CCT, PFD acts on TRiC/CCT-substrate complex to enhance the rate of the folding reaction. PFD alternates between an open latched conformation and a closed engaged conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC binds its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates |
756368 |
