Title : Discovery of a potential allosteric ligand binding site in CDK2.

Pub. Date : 2011 May 20

PMID : 21291269






4 Functional Relationships(s)
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1 In an effort to identify potential target sites for disruption of the CDK-cyclin interaction, we probed the extrinsic fluorophore 8-anilino-1-naphthalene sulfonate (ANS) with human CDK2 and cyclin A using fluorescence spectroscopy and protein crystallography. 8-anilino-1-naphthalenesulfonic acid cyclin A2 Homo sapiens
2 In an effort to identify potential target sites for disruption of the CDK-cyclin interaction, we probed the extrinsic fluorophore 8-anilino-1-naphthalene sulfonate (ANS) with human CDK2 and cyclin A using fluorescence spectroscopy and protein crystallography. 8-anilino-1-naphthalenesulfonic acid cyclin A2 Homo sapiens
3 ANS interacts with free CDK2 in a saturation-dependent manner with an apparent K(d) of 37 muM, and cyclin A displaced ANS from CDK2 with an EC(50) value of 0.6 muM. 8-anilino-1-naphthalenesulfonic acid cyclin A2 Homo sapiens
4 Binding of ANS is accompanied by substantial structural changes in CDK2, resulting in a C-helix conformation that is incompatible for cyclin A association. 8-anilino-1-naphthalenesulfonic acid cyclin A2 Homo sapiens