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. 2015 Apr 24;16(5):9314–9340. doi: 10.3390/ijms16059314

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Comparison of the CDK2 conformation changes in free, partially and fully activated states. (A) Structural superposition of free and partially activated CDK2 complexes; (B) The alignment of partially and fully activated CDK2 complexes; (C) Structural superposition of free and fully activated CDK2 complexes. The yellow, pink and cyan patterns indicate the monomeric CDK2 (free state, coordinates 1HCK), CDK2/cyclin A complex (partially activated form, 1FIN) and phosphorylated dimer (fully activated state, 4EOM), respectively. The changed conformations of monomeric CDK2, CDK2/cyclin A complex and phosphorylated dimer are colored in orange, magenta and blue, respectively.