Molekulová dynamika CDK2 se substrátovým peptidem HHASPRK, inhibice fosforylací

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002046" target="_blank" >RIV/61989592:15310/04:00002046 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation

Popis výsledku v původním jazyce

The cyclin-dependent kinase-2, CDK2, controls the eukaryotic cell cycle at the G1 -S boundary. CDK2 catalyzes the phosphoryl transfer of the adenosine-5´-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatorysubunit (Cyclin A or Cyclin E) and phosphorylation at positive regulatory site in the activation segment (T-loop)1. The CDK2 activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various artificial and natural protein inhibitors2,3, etc. The CDK2 can be also negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 residue in the inhibition segment (G-loop)4. Mechanism of the CDK2 inhibition by phosphorylation is known from the kinetics experiments but the structural aspects of inhibition remains unclear. The first attempt to explain the mechanism of inhibition by phosphorylation came from molecula

Název v anglickém jazyce

A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation

Popis výsledku anglicky

The cyclin-dependent kinase-2, CDK2, controls the eukaryotic cell cycle at the G1 -S boundary. CDK2 catalyzes the phosphoryl transfer of the adenosine-5´-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatorysubunit (Cyclin A or Cyclin E) and phosphorylation at positive regulatory site in the activation segment (T-loop)1. The CDK2 activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various artificial and natural protein inhibitors2,3, etc. The CDK2 can be also negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 residue in the inhibition segment (G-loop)4. Mechanism of the CDK2 inhibition by phosphorylation is known from the kinetics experiments but the structural aspects of inhibition remains unclear. The first attempt to explain the mechanism of inhibition by phosphorylation came from molecula

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

Suppl.

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

260

Kód UT WoS článku

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EID výsledku v databázi Scopus

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