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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F06%3A00016379%21RIV10-MSM-14310___
rdf:type
n14:Vysledek skos:Concept
dcterms:description
We have used molecular dynamics to help understanding different mechanism of CDK2 and CDK5 activation and inhibition. The data were obtained from several simulations including fully active CDK2 in a complex with a short peptide substrate. and simulations on CDK5 in complexes with the protein activator p25 and the purine-like inhibitor roscovitine. Differences between the CDK5/p25 and CDK2/Cyclin A systems are discussed with respect to their specific functionality. We will show why the CDK2 inhibition segment becomes an activation segment for CDK5. We will also clarify why only one step is necessary to activate CDK5 (interaction with the regulatory subunit) while CDK2 needs a two-step activation (other phosphorylation in the activation loop). As a “side effect” information obtained from simulations, we will show how a detailed analysis of the interactions between the protein and the solvent could be used to design new inhibitors. We have used molecular dynamics to help understanding different mechanism of CDK2 and CDK5 activation and inhibition. The data were obtained from several simulations including fully active CDK2 in a complex with a short peptide substrate. and simulations on CDK5 in complexes with the protein activator p25 and the purine-like inhibitor roscovitine. Differences between the CDK5/p25 and CDK2/Cyclin A systems are discussed with respect to their specific functionality. We will show why the CDK2 inhibition segment becomes an activation segment for CDK5. We will also clarify why only one step is necessary to activate CDK5 (interaction with the regulatory subunit) while CDK2 needs a two-step activation (other phosphorylation in the activation loop). As a “side effect” information obtained from simulations, we will show how a detailed analysis of the interactions between the protein and the solvent could be used to design new inhibitors.
dcterms:title
THE ROLE OF PHOSPHORYLATION IN CYCLIN DEPENDENT KINASE 2 AND 5 ACTIVATION AND INHIBITION. A COMPUTER SIMULATION STUDY. THE ROLE OF PHOSPHORYLATION IN CYCLIN DEPENDENT KINASE 2 AND 5 ACTIVATION AND INHIBITION. A COMPUTER SIMULATION STUDY.
skos:prefLabel
THE ROLE OF PHOSPHORYLATION IN CYCLIN DEPENDENT KINASE 2 AND 5 ACTIVATION AND INHIBITION. A COMPUTER SIMULATION STUDY. THE ROLE OF PHOSPHORYLATION IN CYCLIN DEPENDENT KINASE 2 AND 5 ACTIVATION AND INHIBITION. A COMPUTER SIMULATION STUDY.
skos:notation
RIV/00216224:14310/06:00016379!RIV10-MSM-14310___
n3:aktivita
n5:P n5:Z
n3:aktivity
P(GD204/03/H016), Z(MSM0021622413)
n3:dodaniDat
n9:2010
n3:domaciTvurceVysledku
n4:9309616 n4:5517680 n4:4347374
n3:druhVysledku
n7:D
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n21:predkladatel
n3:idSjednocenehoVysledku
497894
n3:idVysledku
RIV/00216224:14310/06:00016379
n3:jazykVysledku
n12:eng
n3:klicovaSlova
phosphorylation cyclin dependent kinase 2 and 5 molecular dynamics
n3:klicoveSlovo
n8:phosphorylation%20cyclin%20dependent%20kinase%202%20and%205%20molecular%20dynamics
n3:kontrolniKodProRIV
[F4706F805DD2]
n3:mistoKonaniAkce
Budapest, Hungary
n3:mistoVydani
Budapest. Hungary
n3:nazevZdroje
1st European Chemistry Congress
n3:obor
n17:CE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n19:GD204%2F03%2FH016
n3:rokUplatneniVysledku
n9:2006
n3:tvurceVysledku
Bártová, Iveta Otyepka, Michal Koča, Jaroslav Kříž, Zdeněk
n3:typAkce
n10:WRD
n3:zahajeniAkce
2006-08-27+02:00
n3:zamer
n18:MSM0021622413
s:numberOfPages
1
n11:hasPublisher
EuCheMS
n20:isbn
963-9319-61-9
n6:organizacniJednotka
14310