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Shared structural features of the 9aaTAD family in complex with CBP

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F15%3A00080651" target="_blank" >RIV/00216224:14110/15:00080651 - isvavai.cz</a>

  • Alternative codes found

    RIV/00843989:_____/15:E0104868

  • Result on the web

    <a href="http://dx.doi.org/10.1039/C4MB00672K" target="_blank" >http://dx.doi.org/10.1039/C4MB00672K</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/C4MB00672K" target="_blank" >10.1039/C4MB00672K</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Shared structural features of the 9aaTAD family in complex with CBP

  • Original language description

    A number of transactivation domains for transcription factors including p53, E2A/HEB, MLL, cMyb, CREB, FOXO3, Gcn4, Oaf1 and Pdr1 have been reported to interact with the KIX domain of general transcriptional mediators CBP, p300 or MED15. Most of those factors belong to the already established Nine amino acid Transactivation Domain (9aaTAD) family. By using available structural data, we found binding analogy for the 9aaTAD in the MLL?KIX and also E2A/HEB?KIX complexes. We recognized two distinct TAD formations in the KIX complex. In the E2A/HEB?KIX complex, the leucine position is determined by the prolonged helical structure including the 9aaTAD and the leucine (long-helical TAD). However in the MLL?KIX complex, the equal position of 9aaTAD and proximal leucine is achieved differently by leucine-turn-helix structural architecture. Furthermore, the FOXO3?KIX complex shares structural analogy with the E2A?KIX complex in respect of both 9aaTAD and proximal leucine.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    ED - Physiology

  • 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)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecular BioSystems

  • ISSN

    1742-206X

  • e-ISSN

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    8

  • Pages from-to

    844-851

  • UT code for WoS article

    000349995600017

  • EID of the result in the Scopus database