<p>Subunits are colored according to nucleotide affinity. Red: high; blue: low. The conformational change may proceed in a sequential fashion owing to the asymmetric usage of ATP by the eukaryotic group II chaperonin. ATP firstly bind to the high ATP affinity hemisphere and induces the conformational change, in less than 1 second. Subsequently, the low ATP affinity hemisphere changes to the closed conformation. Finally, the ring rotates in counter clockwise direction by the cooperative action of the subunits in the ring.</p
<p>More intense colors (blue for domain C1 and red for domain C2) correspond to larger movements com...
<p><b>(A)</b> The binding direction of the ATP-Mg<sup>2+</sup> complex. In the PDB file, the PA, PB ...
To reach a functional and energetically stable conformation, many proteins need molecular helpers ca...
The type II chaperonin CCT (chaperonin containing Tcp-1) of eukaryotic cytosol is a heteromeric 16-m...
The eukaryotic cytoplasmic chaperonin containing TCP-1 (CCT) is a hetero-oligomeric complex that ass...
Background: The chaperonins, a family of molecular chaperones, are large oligomeric proteins that bi...
<div><p>The eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT),...
The eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT), plays a...
Folding to completion of actin and tubulin in the eukaryotic cytosol requires their interaction with...
The rotational mechanism of ATP synthases requires a unique interface between the stator a subunit a...
The eukaryotic cytosolic chaperonin CCT (chaperonin containing TCP-1) is the most complex of all cha...
<p>A-C. Domain movements. The AMPPNP-bound form is colored in red, while the apo-form is colored in ...
The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar ...
<div><p>Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol a...
The cytosolic chaperonin CCT is a 1-MDa protein-folding machine essential for eukaryotic life. The C...
<p>More intense colors (blue for domain C1 and red for domain C2) correspond to larger movements com...
<p><b>(A)</b> The binding direction of the ATP-Mg<sup>2+</sup> complex. In the PDB file, the PA, PB ...
To reach a functional and energetically stable conformation, many proteins need molecular helpers ca...
The type II chaperonin CCT (chaperonin containing Tcp-1) of eukaryotic cytosol is a heteromeric 16-m...
The eukaryotic cytoplasmic chaperonin containing TCP-1 (CCT) is a hetero-oligomeric complex that ass...
Background: The chaperonins, a family of molecular chaperones, are large oligomeric proteins that bi...
<div><p>The eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT),...
The eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT), plays a...
Folding to completion of actin and tubulin in the eukaryotic cytosol requires their interaction with...
The rotational mechanism of ATP synthases requires a unique interface between the stator a subunit a...
The eukaryotic cytosolic chaperonin CCT (chaperonin containing TCP-1) is the most complex of all cha...
<p>A-C. Domain movements. The AMPPNP-bound form is colored in red, while the apo-form is colored in ...
The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar ...
<div><p>Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol a...
The cytosolic chaperonin CCT is a 1-MDa protein-folding machine essential for eukaryotic life. The C...
<p>More intense colors (blue for domain C1 and red for domain C2) correspond to larger movements com...
<p><b>(A)</b> The binding direction of the ATP-Mg<sup>2+</sup> complex. In the PDB file, the PA, PB ...
To reach a functional and energetically stable conformation, many proteins need molecular helpers ca...