COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00009258" target="_blank" >RIV/00216224:14310/03:00009258 - 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

COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION

Popis výsledku v původním jazyce

Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sitesat Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxylin the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is

Název v anglickém jazyce

COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION

Popis výsledku anglicky

Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sitesat Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxylin the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is

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

Book of Abstracts

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

8

Název nakladatele

Workshop on Modeling Interactions in Biomolecules

Místo vydání

Praha

Místo konání akce

Nové Hrady

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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