Molecular Dynamics Simulations of CDK2/ATP Complex

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Publikace nespadá pod Lékařskou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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BÁRTOVÁ Iveta KŘÍŽ Zdeněk OTYEPKA Michal KOČA Jaroslav

Rok publikování 2002
Druh Článek ve sborníku
Konference Chemicke listy 6
Fakulta / Pracoviště MU

Přírodovědecká fakulta

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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