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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F02%3A00007235%21RIV08-MSM-14310___
rdf:type
n10:Vysledek skos:Concept
dcterms:description
Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. This is tightly regulated by the activity of CDKs. A CDK enzyme consists typically of a catalytic subunit, kinase, and a regulatory subunit, cyclin. CDKs are inactive as monomers. For activation requires binding to cyclins. Full activity CDKs obtain at binding with adenosine triphosphate (ATP) by phosphorylation of a threonine residue in the CDK [3]. Activity of these enzymes are inhibited in several ways, for examples, (de)phosphorylation, interaction with various natural protein inhibitors. This work describes behavior of CDK2/ATP complex using the molecular dynamics simulations with the Cornell et al. force field as implemented in the AMBER software package. Results of conformational behavior of ATP in CDK2/ATP complex will be presented. The interaction energies calculated between ATP and amino acids in the active site show the residues that are important for substrate recognition. The binding energie of ATP were cal Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. This is tightly regulated by the activity of CDKs. A CDK enzyme consists typically of a catalytic subunit, kinase, and a regulatory subunit, cyclin. CDKs are inactive as monomers. For activation requires binding to cyclins. Full activity CDKs obtain at binding with adenosine triphosphate (ATP) by phosphorylation of a threonine residue in the CDK [3]. Activity of these enzymes are inhibited in several ways, for examples, (de)phosphorylation, interaction with various natural protein inhibitors. This work describes behavior of CDK2/ATP complex using the molecular dynamics simulations with the Cornell et al. force field as implemented in the AMBER software package. Results of conformational behavior of ATP in CDK2/ATP complex will be presented. The interaction energies calculated between ATP and amino acids in the active site show the residues that are important for substrate recognition. The binding energie of ATP were cal Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. This is tightly regulated by the activity of CDKs. A CDK enzyme consists typically of a catalytic subunit, kinase, and a regulatory subunit, cyclin. CDKs are inactive as monomers. For activation requires binding to cyclins. Full activity CDKs obtain at binding with adenosine triphosphate (ATP) by phosphorylation of a threonine residue in the CDK [3]. Activity of these enzymes are inhibited in several ways, for examples, (de)phosphorylation, interaction with various natural protein inhibitors. This work describes behavior of CDK2/ATP complex using the molecular dynamics simulations with the Cornell et al. force field as implemented in the AMBER software package. Results of conformational behavior of ATP in CDK2/ATP complex will be presented. The interaction energies calculated between ATP and amino acids in the active site show the residues that are important for substrate recognition. The binding energie of ATP were cal
dcterms:title
Molecular Dynamics Simulations of CDK2/ATP Complex Molecular Dynamics Simulations of CDK2/ATP Complex Molecular Dynamics Simulations of CDK2/ATP Complex
skos:prefLabel
Molecular Dynamics Simulations of CDK2/ATP Complex Molecular Dynamics Simulations of CDK2/ATP Complex Molecular Dynamics Simulations of CDK2/ATP Complex
skos:notation
RIV/00216224:14310/02:00007235!RIV08-MSM-14310___
n3:strany
427
n3:aktivita
n11:P
n3:aktivity
P(LN00A016)
n3:dodaniDat
n5:2008
n3:domaciTvurceVysledku
n18:9309616 n18:4347374 n18:5517680
n3:druhVysledku
n17:D
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n20:predkladatel
n3:idSjednocenehoVysledku
654099
n3:idVysledku
RIV/00216224:14310/02:00007235
n3:jazykVysledku
n16:eng
n3:klicovaSlova
Cyclin dependent kinase; ATP; Molecular dynamics
n3:klicoveSlovo
n8:Cyclin%20dependent%20kinase n8:Molecular%20dynamics n8:ATP
n3:kontrolniKodProRIV
[B77ADF5355CF]
n3:mistoKonaniAkce
Brno
n3:mistoVydani
Praha
n3:nazevZdroje
Chemicke listy 6
n3:obor
n13:BO
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n12:LN00A016
n3:rokUplatneniVysledku
n5:2002
n3:tvurceVysledku
Kříž, Zdeněk Bártová, Iveta Koča, Jaroslav Otyepka, Michal
n3:typAkce
n6:EUR
n3:zahajeniAkce
2002-01-01+01:00
s:numberOfPages
1
n19:hasPublisher
54. Sjezd chemickych spolecnosti
n15:organizacniJednotka
14310