A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00009964" target="_blank" >RIV/00216224:14310/04:00009964 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

čeština

Název v původním jazyce

A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation

Popis výsledku v původním jazyce

The cyclin-dependent kinase, CDK2, regulates the eukaryotic cell cycle at the G1; S boundary. CDKs activity is regulated by complex mechanism including binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. For activation CDK2 requires binding to Cyclin A or Cyclin E. The CDK2 obtains full activity after phosphorylation of the threonine residue (T160) in the activation segment (T-loop) [2]. CDK2 catalyzes the phosphoryl transfer of the adenosine-5-triphosphate (ATP) g-phosphate to serine or threonine hydroxyl in the protein substrate. The CDKs activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various natural protein inhibitors [3,4], etc. The CDK2 can be negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 in the glycine-rich loop (G-loop) [5]. This work describes behavior of the fully active CDK2 (pT160-CDK2/Cyclin A/ATP complex) with substrate peptide (HHASPRK) a

Název v anglickém jazyce

A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation

Popis výsledku anglicky

The cyclin-dependent kinase, CDK2, regulates the eukaryotic cell cycle at the G1; S boundary. CDKs activity is regulated by complex mechanism including binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. For activation CDK2 requires binding to Cyclin A or Cyclin E. The CDK2 obtains full activity after phosphorylation of the threonine residue (T160) in the activation segment (T-loop) [2]. CDK2 catalyzes the phosphoryl transfer of the adenosine-5-triphosphate (ATP) g-phosphate to serine or threonine hydroxyl in the protein substrate. The CDKs activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various natural protein inhibitors [3,4], etc. The CDK2 can be negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 in the glycine-rich loop (G-loop) [5]. This work describes behavior of the fully active CDK2 (pT160-CDK2/Cyclin A/ATP complex) with substrate peptide (HHASPRK) a

Druh

D - Stať ve sborníku

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

Materials in Structure Chemistry, Biology, Physics and Technology

ISBN

1211 - 5894

ISSN

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e-ISSN

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Počet stran výsledku

2

Strana od-do

42-43

Název nakladatele

Krystalografická společnost

Místo vydání

Praha

Místo konání akce

Nové Hrady

Datum konání akce

11. 3. 2004

Typ akce podle státní příslušnosti

CST - Celostátní akce

Kód UT WoS článku

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