Cyclin-dependent kinases (CDKs) are mostly known for their role in the cell cycle regulation. The activation mechanism of all CDKs involves the association with a regulatory protein, generally a cyclin, that binds to the kinase unit and stabilizes a catalytically active conformation. Active and inactive conformations of CDKs are characterized by the different spatial localization of two typical elements, namely the activation loop and an -helix, whose amino-acid composition varies throughout the family.
Cavalli A., Berteotti A., Branduardi D., Gervasio F.L., Recanatini M., Parrinello M. (2007). Protein Conformational Plasticity: the “off-on” Switching Movement in Cdk5. MELVILLE : American Institute of Physics.
Protein Conformational Plasticity: the “off-on” Switching Movement in Cdk5
CAVALLI, ANDREA;RECANATINI, MAURIZIO;
2007
Abstract
Cyclin-dependent kinases (CDKs) are mostly known for their role in the cell cycle regulation. The activation mechanism of all CDKs involves the association with a regulatory protein, generally a cyclin, that binds to the kinase unit and stabilizes a catalytically active conformation. Active and inactive conformations of CDKs are characterized by the different spatial localization of two typical elements, namely the activation loop and an -helix, whose amino-acid composition varies throughout the family.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
