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Structural Basis for CDK Activation

Binding of the corresponding cyclin and activating phosphorylation are required for full activation of the CDKs. Without the cyclin, the CDKs are inactive the CDK-cyclin complex possesses a basal protein kinase activity that is considerably increased by phosphorylation at Thr in position 160 (or equivalent position). The structural changes [Pg.396]

It is assumed that the activity increase is mainly due to better accessibility of the binding site for the protein substrate. In the unphosphorylated form, the T loop blocks access to the substrate binding site whereas in the phosphorylated form, this site is exposed. [Pg.398]


See other pages where Structural Basis for CDK Activation is mentioned: [Pg.396]    [Pg.442]    [Pg.552]   


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Structural Basis

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