Editing Cyclin-dependent kinase complex (section)

=== αC-Helix ===
The αC-Helix region is highly conserved across many of the mammalian kinome (family of [[Kinase|kinases]]). Its main responsibility is to maintain [[Allosteric regulation|allosteric control]] of the kinase active site. This control manifests in CDK-cyclin complexes by specifically preventing CDK activity until its binds to its partner regulator (i.e. cyclin or other partner protein). This binding causes a conformational change in the αC-Helix region of the CDK and allows for it to be moved from the active site cleft and completes the initial process of T-loop activation. Given that this region is so conserved across the protein superfamily of kinases, this mechanism where the αC-Helix has been shown to fold out of the N-terminal lobe of the kinase, allowing for increased access to the αL-12 Helix that lies within the T-loop, is considered a potential target for drug development.<ref>Lorenzo Palmieri, Giulio Rastelli, αC helix displacement as a general approach for allosteric modulation of protein kinases, Drug Discovery Today, Volume 18, Issues 7–8, 2013, Pages 407-414, ISSN 1359-6446, {{doi|10.1016/j.drudis.2012.11.009}}.</ref>