Cyclin-Dependent Protein Kinase-2 Regulation by Phosphorylation, A Molecular Dynamics Study

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00009259" target="_blank" >RIV/00216224:14310/03:00009259 - 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

Cyclin-Dependent Protein Kinase-2 Regulation by Phosphorylation, A Molecular Dynamics Study

Popis výsledku v původním jazyce

Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. CDKs activity is regulated by complex mechanism that include binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. CDK2 requires for activation binding to cyclinA or cyclinE. CDK2 obtains full activity by phosphorylation of the Thr160 residue in the activation segment (T-loop) [2]. CDKs activity is natively inhibited in several ways, for example, by (de)phosphorylation, interactions with various natural protein inhibitors [3], etc. CDK2 can be negatively regulated by phosphorylation at Tyr15 and (theoretically) at Thr14 [4]. Human CDK2 contains the classical bi-lobal kinase fold [1]. The N-terminal domain is composedmainly of b-sheet, containing five anti-parallel b-strands, and one helix (the C-helix). The larger C-terminal domain is predominantly a-helical, and is linked to the N-terminal domain by a flexible hinge (see picture). The adenosine tri

Název v anglickém jazyce

Cyclin-Dependent Protein Kinase-2 Regulation by Phosphorylation, A Molecular Dynamics Study

Popis výsledku anglicky

Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. CDKs activity is regulated by complex mechanism that include binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. CDK2 requires for activation binding to cyclinA or cyclinE. CDK2 obtains full activity by phosphorylation of the Thr160 residue in the activation segment (T-loop) [2]. CDKs activity is natively inhibited in several ways, for example, by (de)phosphorylation, interactions with various natural protein inhibitors [3], etc. CDK2 can be negatively regulated by phosphorylation at Tyr15 and (theoretically) at Thr14 [4]. Human CDK2 contains the classical bi-lobal kinase fold [1]. The N-terminal domain is composedmainly of b-sheet, containing five anti-parallel b-strands, and one helix (the C-helix). The larger C-terminal domain is predominantly a-helical, and is linked to the N-terminal domain by a flexible hinge (see picture). The adenosine tri

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

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

Cellular and Molecular Biology Letters

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

2

Strana od-do

574-575

Název nakladatele

3rd International Conference Inhibitors of Protein Kinases

Místo vydání

Wroclav

Místo konání akce

Warsaw

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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