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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F04%3A00009964%21RIV%2F2005%2FMSM%2F143105%2FN
rdf:type
n12:Vysledek skos:Concept
dcterms:description
The cyclin-dependent kinase, CDK2, regulates the eukaryotic cell cycle at the G1; S boundary. CDKs activity is regulated by complex mechanism including binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. For activation CDK2 requires binding to Cyclin A or Cyclin E. The CDK2 obtains full activity after phosphorylation of the threonine residue (T160) in the activation segment (T-loop) [2]. CDK2 catalyzes the phosphoryl transfer of the adenosine-5-triphosphate (ATP) g-phosphate to serine or threonine hydroxyl in the protein substrate. The CDKs activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various natural protein inhibitors [3,4], etc. The CDK2 can be negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 in the glycine-rich loop (G-loop) [5]. This work describes behavior of the fully active CDK2 (pT160-CDK2/Cyclin A/ATP complex) with substrate peptide (HHASPRK) and CDK2 inhibit The cyclin-dependent kinase, CDK2, regulates the eukaryotic cell cycle at the G1; S boundary. CDKs activity is regulated by complex mechanism including binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. For activation CDK2 requires binding to Cyclin A or Cyclin E. The CDK2 obtains full activity after phosphorylation of the threonine residue (T160) in the activation segment (T-loop) [2]. CDK2 catalyzes the phosphoryl transfer of the adenosine-5-triphosphate (ATP) g-phosphate to serine or threonine hydroxyl in the protein substrate. The CDKs activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various natural protein inhibitors [3,4], etc. The CDK2 can be negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 in the glycine-rich loop (G-loop) [5]. This work describes behavior of the fully active CDK2 (pT160-CDK2/Cyclin A/ATP complex) with substrate peptide (HHASPRK) and CDK2 inhibit The cyclin-dependent kinase, CDK2, regulates the eukaryotic cell cycle at the G1; S boundary. CDKs activity is regulated by complex mechanism including binding to positive regulatory subunit and phosphorylation at positive and/or negative regulatory sites [1]. For activation CDK2 requires binding to Cyclin A or Cyclin E. The CDK2 obtains full activity after phosphorylation of the threonine residue (T160) in the activation segment (T-loop) [2]. CDK2 catalyzes the phosphoryl transfer of the adenosine-5-triphosphate (ATP) g-phosphate to serine or threonine hydroxyl in the protein substrate. The CDKs activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various natural protein inhibitors [3,4], etc. The CDK2 can be negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 in the glycine-rich loop (G-loop) [5]. This work describes behavior of the fully active CDK2 (pT160-CDK2/Cyclin A/ATP complex) with substrate peptide (HHASPRK) and CDK2 inhibit
dcterms:title
A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation
skos:prefLabel
A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation A Molecular Dynamics Study of the Cyclin-Dependent Kinase-2 (CDK2) with Substrate Peptide (HHASPRK), Inhibition of CDK2 by Phosphorylation
skos:notation
RIV/00216224:14310/04:00009964!RIV/2005/MSM/143105/N
n3:strany
42-43
n3:aktivita
n10:P
n3:aktivity
P(LN00A016)
n3:dodaniDat
n18:2005
n3:domaciTvurceVysledku
n8:5517680 n8:9309616 n8:4347374
n3:druhVysledku
n4:D
n3:duvernostUdaju
n13:S
n3:entitaPredkladatele
n9:predkladatel
n3:idSjednocenehoVysledku
552988
n3:idVysledku
RIV/00216224:14310/04:00009964
n3:jazykVysledku
n16:cze
n3:klicovaSlova
Cyclin dependent kinase, inhibition, phosphorylation, molecular dynamics
n3:klicoveSlovo
n15:molecular%20dynamics n15:phosphorylation n15:inhibition n15:Cyclin%20dependent%20kinase
n3:kontrolniKodProRIV
[BD9AFCDC07DC]
n3:mistoKonaniAkce
Nové Hrady
n3:mistoVydani
Praha
n3:nazevZdroje
Materials in Structure Chemistry, Biology, Physics and Technology
n3:obor
n14:CF
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n17:LN00A016
n3:rokUplatneniVysledku
n18:2004
n3:tvurceVysledku
Koča, Jaroslav Kříž, Zdeněk Otyepka, Michal Bártová, Iveta
n3:typAkce
n20:CST
n3:zahajeniAkce
2004-03-11+01:00
s:issn
1211-5894
s:numberOfPages
2
n19:hasPublisher
Krystalografická společnost
n11:organizacniJednotka
14310