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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F06%3A00015728%21RIV10-MSM-14310___
rdf:type
n13:Vysledek skos:Concept
dcterms:description
A detailed analysis is presented of the dynamics of human CDK5 in complexes with the protein activator p25 and the purine-like inhibitor roscovitine. These, and other findings related to the activation of CDK5 are critically reviewed from a molecular perspective. In addition, the results obtained on the behavior of CDK5 are compared to data on CDK2 to assess the differences and similarities between the two kinases in terms of (i) roscovitine binding, (ii) regulatory subunit association, (iii) conformational changes in the T-loop following CDK/regulatory subunit complex formation and (iv) specificity in CDK/regulatory subunit recognition. An energy decomposition analysis, used for these purposes, revealed why the binding of p25 alone is sufficient to stabilize the extended active T-loop conformation of CDK5, whereas the equivalent conformational change in CDK2 requires both the binding of Cyclin A and phosphorylation of the Thr160 residue. A detailed analysis is presented of the dynamics of human CDK5 in complexes with the protein activator p25 and the purine-like inhibitor roscovitine. These, and other findings related to the activation of CDK5 are critically reviewed from a molecular perspective. In addition, the results obtained on the behavior of CDK5 are compared to data on CDK2 to assess the differences and similarities between the two kinases in terms of (i) roscovitine binding, (ii) regulatory subunit association, (iii) conformational changes in the T-loop following CDK/regulatory subunit complex formation and (iv) specificity in CDK/regulatory subunit recognition. An energy decomposition analysis, used for these purposes, revealed why the binding of p25 alone is sufficient to stabilize the extended active T-loop conformation of CDK5, whereas the equivalent conformational change in CDK2 requires both the binding of Cyclin A and phosphorylation of the Thr160 residue.
dcterms:title
DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS
skos:prefLabel
DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS
skos:notation
RIV/00216224:14310/06:00015728!RIV10-MSM-14310___
n3:aktivita
n14:P n14:Z
n3:aktivity
P(GD204/03/H016), P(LC512), Z(MSM0021622413), Z(MSM6198959216)
n3:cisloPeriodika
11
n3:dodaniDat
n9:2010
n3:domaciTvurceVysledku
n11:5517680 n11:9309616 n11:4347374
n3:druhVysledku
n15:J
n3:duvernostUdaju
n19:S
n3:entitaPredkladatele
n4:predkladatel
n3:idSjednocenehoVysledku
471632
n3:idVysledku
RIV/00216224:14310/06:00015728
n3:jazykVysledku
n8:eng
n3:klicovaSlova
cell cycle; CDK5 regulation; CDK2 regulation; glycine?rich loop; CDK dynamics
n3:klicoveSlovo
n12:glycine%3Frich%20loop n12:cell%20cycle n12:CDK%20dynamics n12:CDK2%20regulation n12:CDK5%20regulation
n3:kodStatuVydavatele
CZ - Česká republika
n3:kontrolniKodProRIV
[D7FC0243E785]
n3:nazevZdroje
The Journal of biological chemistry
n3:obor
n17:CF
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n5:LC512 n5:GD204%2F03%2FH016
n3:rokUplatneniVysledku
n9:2006
n3:svazekPeriodika
281
n3:tvurceVysledku
Bártová, Iveta Otyepka, Michal Koča, Jaroslav Kříž, Zdeněk
n3:zamer
n18:MSM6198959216 n18:MSM0021622413
s:issn
0021-9258
s:numberOfPages
11
n16:organizacniJednotka
14310