2cjm

File:2cjm.gif

spinqualitylabelsall models 2cjm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE

OverviewOverview

Inhibition of cyclin-dependent kinase 1 (CDK1) activity by Tyr-15, phosphorylation directly regulates entry into mitosis and is an important, element in the control of the unperturbed cell cycle. Active site, phosphorylation of other members of the CDK family that regulate cell, cycle progression instates checkpoints that are fundamental to eukaryotic, cell cycle regulation. Kinetic and crystallographic analyses of, CDK2-cyclin A complexes reveal that this inhibitory mechanism operates, through steric blockade of peptide substrate binding and through the, creation of an environment that favors a non-productive conformation of, the terminal group of ATP. By contrast, tyrosine phosphorylation of CDK2, alters neither its Km for ATP nor its significant intrinsic ATPase, activity. ... [(full description)]

About this StructureAbout this Structure

2CJM is a [Protein complex] structure of sequences from [Homo sapiens] with MG, PTR and ATP as [ligands]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].

ReferenceReference

How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A., Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA, J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:17095507

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