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

Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Cyclin-Dependent Protein Kinase-2 Regulation by Phosphorylation, A Molecular Dynamics Study
Original language description
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
Czech name
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Czech description
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Project
<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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