1e9h
THR 160 PHOSPHORYLATED CDK2-HUMAN CYCLIN A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-SULPHONATE BOUND
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OverviewOverview
BACKGROUND: Cyclin-dependent kinase 2 (CDK2) is an important target for, structure-based design of antitumor agents. Monomeric CDK2 is inactive., Activation requires rearrangements to key structural elements of the, enzyme's active site, which accompany cyclin binding and phosphorylation., To assess the validity of using monomeric CDK2 as a model for the active, kinase in structure-based drug design, we have solved the structure of the, inhibitor indirubin-5-sulphonate (E226) complexed with phospho-CDK2-cyclin, A and compared it with the structure of E226 bound to inactive, monomeric, CDK2. RESULTS: Activation of monomeric CDK2 leads to a rotation of its, N-terminal domain relative to the C-terminal lobe. The accompanying change, in position of E226 follows that of the N-terminal domain, ... [(full description)]
About this StructureAbout this Structure
1E9H is a [Protein complex] structure of sequences from [Homo sapiens] with INR as [ligand]. Active as [Transferred entry: 2.7.11.1], with EC number [2.7.1.37]. Structure known Active Site: INA. Full crystallographic information is available from [OCA].
ReferenceReference
Inhibitor binding to active and inactive CDK2: the crystal structure of CDK2-cyclin A/indirubin-5-sulphonate., Davies TG, Tunnah P, Meijer L, Marko D, Eisenbrand G, Endicott JA, Noble ME, Structure. 2001 May 9;9(5):389-97. PMID:11377199
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