Pub. Date : 2011 May 20
PMID : 21291269
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 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 dependent kinase 2 | 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 dependent kinase 2 | 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 dependent kinase 2 | Homo sapiens |
| 4 | 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 dependent kinase 2 | Homo sapiens |
| 5 | 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 dependent kinase 2 | Homo sapiens |
| 6 | These findings indicate the potential of the ANS binding pocket as a new target site for allosteric inhibitors disrupting the interaction of CDKs and cyclins. | 8-anilino-1-naphthalenesulfonic acid | cyclin dependent kinase 2 | Homo sapiens |