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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F02%3A00006680%21RIV08-GA0-14310___
rdf:type
n16:Vysledek skos:Concept
dcterms:description
This article presents a molecular dynamics (MD) study of the cdk2 enzyme and its two complexes with the inhibitors isopentenyladenine and roscovitine using the Cornell et at. force field from the AMBER software package. The results show that inserting an inhibitor into the enzyme active site does not considerably change enzyme structure but it seemingly changes the distribution of internal motions. The inhibitor causes differences in the domain motions in free cdk2 and in its complexes. It was found out that repulsion of roscovitine N9 substituent causes conformational change on Lys 33 side chain. Isopentenyladenine forms with Lys 33 side chain terminal amino group a hydrogen bond. It implies that the cavity, where N9 substituent of roscovitine is buried, can adopt larger substituent due to Lys 33 side chain flexibility. The composition of electrostatic and van der Waals interactions between the inhibitor and the enzyme were also calculated along both cdk2/inhibitor MD trajectories together with MM-PB This article presents a molecular dynamics (MD) study of the cdk2 enzyme and its two complexes with the inhibitors isopentenyladenine and roscovitine using the Cornell et at. force field from the AMBER software package. The results show that inserting an inhibitor into the enzyme active site does not considerably change enzyme structure but it seemingly changes the distribution of internal motions. The inhibitor causes differences in the domain motions in free cdk2 and in its complexes. It was found out that repulsion of roscovitine N9 substituent causes conformational change on Lys 33 side chain. Isopentenyladenine forms with Lys 33 side chain terminal amino group a hydrogen bond. It implies that the cavity, where N9 substituent of roscovitine is buried, can adopt larger substituent due to Lys 33 side chain flexibility. The composition of electrostatic and van der Waals interactions between the inhibitor and the enzyme were also calculated along both cdk2/inhibitor MD trajectories together with MM-PB This article presents a molecular dynamics (MD) study of the cdk2 enzyme and its two complexes with the inhibitors isopentenyladenine and roscovitine using the Cornell et at. force field from the AMBER software package. The results show that inserting an inhibitor into the enzyme active site does not considerably change enzyme structure but it seemingly changes the distribution of internal motions. The inhibitor causes differences in the domain motions in free cdk2 and in its complexes. It was found out that repulsion of roscovitine N9 substituent causes conformational change on Lys 33 side chain. Isopentenyladenine forms with Lys 33 side chain terminal amino group a hydrogen bond. It implies that the cavity, where N9 substituent of roscovitine is buried, can adopt larger substituent due to Lys 33 side chain flexibility. The composition of electrostatic and van der Waals interactions between the inhibitor and the enzyme were also calculated along both cdk2/inhibitor MD trajectories together with MM-PB
dcterms:title
Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations
skos:prefLabel
Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations
skos:notation
RIV/00216224:14310/02:00006680!RIV08-GA0-14310___
n3:strany
141
n3:aktivita
n17:P
n3:aktivity
P(GV201/98/K041), P(LN00A016)
n3:cisloPeriodika
2
n3:dodaniDat
n13:2008
n3:domaciTvurceVysledku
n4:4347374 n4:9309616
n3:druhVysledku
n15:J
n3:duvernostUdaju
n14:S
n3:entitaPredkladatele
n6:predkladatel
n3:idSjednocenehoVysledku
643875
n3:idVysledku
RIV/00216224:14310/02:00006680
n3:jazykVysledku
n5:eng
n3:klicovaSlova
cyclin dependent kinase; drug design; inhibitors; molecular dynamics; roscovitine
n3:klicoveSlovo
n8:molecular%20dynamics n8:inhibitors n8:cyclin%20dependent%20kinase n8:roscovitine n8:drug%20design
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[CC68843C03F0]
n3:nazevZdroje
Journal of Biomolecular Structure & Dynamics
n3:obor
n10:BO
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
3
n3:projekt
n7:GV201%2F98%2FK041 n7:LN00A016
n3:rokUplatneniVysledku
n13:2002
n3:svazekPeriodika
20
n3:tvurceVysledku
Otyepka, Michal Kříž, Zdeněk Koča, Jaroslav
s:issn
0739-1102
s:numberOfPages
14
n18:organizacniJednotka
14310