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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F04%3A00010530%21RIV08-MSM-14310___
rdf:type
n7:Vysledek skos:Concept
dcterms:description
Nanoseconds long molecular dynamics (MD) trajectories of differently active complexes of human cyclin-dependent kinase 2 (inactive CDK2/ATP, semi-active CDK2/Cyclin A/ATP, fully-active pT160-CDK2/Cyclin A/ATP, inhibited pT14-; pY15-; and pT14,pY15,pT160-CDK2/Cyclin A/ATP) are compared. The MD simulations results of CDK2 inhibition by phosphorylation at T14 and/or Y15 sites provide insight into structural aspects of CDK2 deactivation. The inhibitory sites are localized in the glycine-rich loop (G-loop) positioned opposite the activation T-loop. Phosphorylation of T14 and both inhibitory sites T14 and Y15 together causes ATP misalignment for phosphorylation and G-loop conformational change. This conformational change leads to the opening of the CDK2 substrate binding box. The phosphorylated Y15 residue negatively affects substrate binding or its correct alignment for ATP terminal phospho-group transfer to the CDK2 substrate. The MD simulations of the CDK2 activation process provide results in agreement Nanoseconds long molecular dynamics (MD) trajectories of differently active complexes of human cyclin-dependent kinase 2 (inactive CDK2/ATP, semi-active CDK2/Cyclin A/ATP, fully-active pT160-CDK2/Cyclin A/ATP, inhibited pT14-; pY15-; and pT14,pY15,pT160-CDK2/Cyclin A/ATP) are compared. The MD simulations results of CDK2 inhibition by phosphorylation at T14 and/or Y15 sites provide insight into structural aspects of CDK2 deactivation. The inhibitory sites are localized in the glycine-rich loop (G-loop) positioned opposite the activation T-loop. Phosphorylation of T14 and both inhibitory sites T14 and Y15 together causes ATP misalignment for phosphorylation and G-loop conformational change. This conformational change leads to the opening of the CDK2 substrate binding box. The phosphorylated Y15 residue negatively affects substrate binding or its correct alignment for ATP terminal phospho-group transfer to the CDK2 substrate. The MD simulations of the CDK2 activation process provide results in agreement Aktivace a Inhibice CDK2
dcterms:title
Activation and Inhibition of Cyclin-Dependent Kinase-2 by Phosphorylation; A Molecular Dynamics Study Reveals the Functional Importance of the Glycine-Rich Loop Activation and Inhibition of Cyclin-Dependent Kinase-2 by Phosphorylation; A Molecular Dynamics Study Reveals the Functional Importance of the Glycine-Rich Loop Aktivace a Inhibice CDK2
skos:prefLabel
Activation and Inhibition of Cyclin-Dependent Kinase-2 by Phosphorylation; A Molecular Dynamics Study Reveals the Functional Importance of the Glycine-Rich Loop Activation and Inhibition of Cyclin-Dependent Kinase-2 by Phosphorylation; A Molecular Dynamics Study Reveals the Functional Importance of the Glycine-Rich Loop Aktivace a Inhibice CDK2
skos:notation
RIV/00216224:14310/04:00010530!RIV08-MSM-14310___
n3:strany
1449-1457
n3:aktivita
n10:Z n10:P
n3:aktivity
P(GV201/98/K041), P(LN00A016), Z(MSM 143100005), Z(MSM 153100007)
n3:cisloPeriodika
6
n3:dodaniDat
n8:2008
n3:domaciTvurceVysledku
n11:4347374 n11:9309616 n11:5517680
n3:druhVysledku
n13:J
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n15:predkladatel
n3:idSjednocenehoVysledku
553442
n3:idVysledku
RIV/00216224:14310/04:00010530
n3:jazykVysledku
n17:eng
n3:klicovaSlova
cell cycle; CDK regulation; phosphorylated tyrosine; threonine
n3:klicoveSlovo
n4:phosphorylated%20tyrosine n4:threonine n4:CDK%20regulation n4:cell%20cycle
n3:kodStatuVydavatele
CZ - Česká republika
n3:kontrolniKodProRIV
[2676DC6AEDDF]
n3:nazevZdroje
Protein Science
n3:obor
n19:CF
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n18:GV201%2F98%2FK041 n18:LN00A016
n3:rokUplatneniVysledku
n8:2004
n3:svazekPeriodika
13
n3:tvurceVysledku
Kříž, Zdeněk Otyepka, Michal Koča, Jaroslav Bártová, Iveta
n3:zamer
n6:MSM%20143100005 n6:MSM%20153100007
s:issn
0961-8368
s:numberOfPages
9
n16:organizacniJednotka
14310