1e9h

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spinqualitylabelsall models 1e9h, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THR 160 PHOSPHORYLATED CDK2-HUMAN CYCLIN A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-SULPHONATE BOUND

Overview

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 Structure

1E9H is a [Protein complex] structure of sequences from [Homo sapiens] with INR as [ligand]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].

Reference

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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