A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation
The result's identifiers
Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation
Original language description
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
Czech name
Molekulová dynamika CDK2 se substrátovým peptidem HHASPRK, inhibice fosforylací
Czech description
Je diskutována molekulová dynamika CDK2 se substrátovým peptidem HHASPRK a inhibice fosforylací.
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
ISSN
0232-0061
e-ISSN
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Volume of the periodical
43
Issue of the periodical within the volume
Suppl.
Country of publishing house
CZ - CZECH REPUBLIC
Number of pages
275
Pages from-to
260
UT code for WoS article
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EID of the result in the Scopus database
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