Molecular Dynamics Simulations of CDK2/ATP Complex
| Autoři | |
|---|---|
| Rok publikování | 2002 |
| Druh | Článek ve sborníku |
| Konference | Chemicke listy 6 |
| Fakulta / Pracoviště MU | |
| Citace | |
| Obor | Biofyzika |
| Klíčová slova | Cyclin dependent kinase; ATP; Molecular dynamics |
| Popis | Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. This is tightly regulated by the activity of CDKs. A CDK enzyme consists typically of a catalytic subunit, kinase, and a regulatory subunit, cyclin. CDKs are inactive as monomers. For activation requires binding to cyclins. Full activity CDKs obtain at binding with adenosine triphosphate (ATP) by phosphorylation of a threonine residue in the CDK [3]. Activity of these enzymes are inhibited in several ways, for examples, (de)phosphorylation, interaction with various natural protein inhibitors. This work describes behavior of CDK2/ATP complex using the molecular dynamics simulations with the Cornell et al. force field as implemented in the AMBER software package. Results of conformational behavior of ATP in CDK2/ATP complex will be presented. The interaction energies calculated between ATP and amino acids in the active site show the residues that are important for substrate recognition. The binding energie of ATP were calculated using MM-PB(GB)SA analysis. The results will be compared with binding energies of two inhibitors (roscovitine and isopentenyladenine) obtained from previous molecular dynamics simulations. |
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