About: The structure and substrate specificity of human Cdk12/Cyclin K

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About: The structure and substrate specificity of human Cdk12/Cyclin K Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.nature.com/ncomms/2014/140324/ncomms4505/pdf/ncomms4505.pdf
Description	Phosphorylation of the RNA polymerase II C-terminal domain (CTD) by cyclin-dependent kinases is important for productive transcription. Here we determine the crystal structure of Cdk12/CycK and analyse its requirements for substrate recognition. Active Cdk12/CycK is arranged in an open conformation similar to that of Cdk9/CycT but different from those of cell cycle kinases. Cdk12 contains a C-terminal extension that folds onto the N- and C-terminal lobes thereby contacting the ATP ribose. The interaction is mediated by an HE motif followed by a polybasic cluster that is conserved in transcriptional CDKs. Cdk12/CycK showed the highest activity on a CTD substrate prephosphorylated at position Ser7, whereas the common Lys7 substitution was not recognized. Flavopiridol is most potent towards Cdk12 but was still 10-fold more potent towards Cdk9. T-loop phosphorylation of Cdk12 required coexpression with a Cdk-activating kinase. Phosphorylation of the RNA polymerase II C-terminal domain (CTD) by cyclin-dependent kinases is important for productive transcription. Here we determine the crystal structure of Cdk12/CycK and analyse its requirements for substrate recognition. Active Cdk12/CycK is arranged in an open conformation similar to that of Cdk9/CycT but different from those of cell cycle kinases. Cdk12 contains a C-terminal extension that folds onto the N- and C-terminal lobes thereby contacting the ATP ribose. The interaction is mediated by an HE motif followed by a polybasic cluster that is conserved in transcriptional CDKs. Cdk12/CycK showed the highest activity on a CTD substrate prephosphorylated at position Ser7, whereas the common Lys7 substitution was not recognized. Flavopiridol is most potent towards Cdk12 but was still 10-fold more potent towards Cdk9. T-loop phosphorylation of Cdk12 required coexpression with a Cdk-activating kinase. (en)
Title	The structure and substrate specificity of human Cdk12/Cyclin K The structure and substrate specificity of human Cdk12/Cyclin K (en)
skos:prefLabel	The structure and substrate specificity of human Cdk12/Cyclin K The structure and substrate specificity of human Cdk12/Cyclin K (en)
skos:notation	RIV/00216224:14740/14:00073691!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(ED1.1.00/02.0068), P(GA14-09979S)
http://linked.open...iv/cisloPeriodika	3505
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Blažek, Dalibor
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	47916
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/14:00073691
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	RNA-POLYMERASE-II; C-TERMINAL DOMAIN; CAPPING ENZYME RECRUITMENT; CYCLIN-DEPENDENT KINASE-9; CTD CODE; P-TEFB; PROTEIN-KINASES; FISSION YEAST; CRYSTAL-STRUCTURE; IN-VIVO (en)
http://linked.open.../riv/klicoveSlovo	RNA-POLYMERASE-II CRYSTAL-STRUCTURE IN-VIVO C-TERMINAL DOMAIN CAPPING ENZYME RECRUITMENT CTD CODE CYCLIN-DEPENDENT KINASE-9 FISSION YEAST P-TEFB PROTEIN-KINASES
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[1C9E5E721972]
http://linked.open...i/riv/nazevZdroje	NATURE COMMUNICATIONS
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	10 (xsd:int)
http://linked.open...vavai/riv/projekt	The role of Cdk12 and C-terminal domain of RNA polymerase II in transcription-coupled genome instability Central european institute of technology
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	5
http://linked.open...iv/tvurceVysledku	Blažek, Dalibor Anand, Kanchan Bösken, Christian A. Eick, Dirk Farnung, Lucas Fisher, Robert P. Geyer, Matthias Hintermair, Corinna Schachter, Miriam Merzel Vogel- Bachmayr, Karin
http://linked.open...ain/vavai/riv/wos	000334302000008
issn	2041-1723
number of pages	14 (xsd:int)
http://bibframe.org/vocab/doi	10.1038/ncomms4505
http://localhost/t...ganizacniJednotka	14740

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