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%2F00216224%3A14310%2F04%3A00010531" target="_blank" >RIV/00216224:14310/04:00010531 - 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 regulatory subunit (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 inhibitors [2,3], 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
Czech name
MD studie CDK2
Czech description
MD studie CDK2
Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
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
Article name in the collection
Acta Univ. Palacki. Olomouc., Fac. Rer. Nat., Chemica 43S
ISBN
80-244-0353-6
ISSN
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e-ISSN
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Number of pages
2
Pages from-to
260-261
Publisher name
Univerzita Palackého
Place of publication
Olomouc
Event location
Olomouc
Event date
Jan 1, 2004
Type of event by nationality
CST - Celostátní akce
UT code for WoS article
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