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The structure and substrate specificity of human Cdk12/Cyclin K

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00073691" target="_blank" >RIV/00216224:14740/14:00073691 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.nature.com/ncomms/2014/140324/ncomms4505/pdf/ncomms4505.pdf" target="_blank" >http://www.nature.com/ncomms/2014/140324/ncomms4505/pdf/ncomms4505.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/ncomms4505" target="_blank" >10.1038/ncomms4505</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The structure and substrate specificity of human Cdk12/Cyclin K

  • Original language 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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2014

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    NATURE COMMUNICATIONS

  • ISSN

    2041-1723

  • e-ISSN

  • Volume of the periodical

    5

  • Issue of the periodical within the volume

    3505

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    14

  • Pages from-to

    "nestránkováno"

  • UT code for WoS article

    000334302000008

  • EID of the result in the Scopus database