All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

NMR characterization of intrinsically disordered microtubule associated protein 2c

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F17%3A00095559" target="_blank" >RIV/00216224:14740/17:00095559 - isvavai.cz</a>

  • Result on the web

    <a href="https://2017.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170093096095093095424170" target="_blank" >https://2017.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170093096095093095424170</a>

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    NMR characterization of intrinsically disordered microtubule associated protein 2c

  • Original language description

    Microtubule-associated protein 2c (MAP2c) is an intrinsically disordered 49kDa protein expressed in developing nerve cells. MAP2c interacts with microtubules, affecting their dynamics, and plays an important role in neuronal morphogenesis. MAP2c function is regulated via phosphorylation by various kinases, including cAMPdependent protein kinase (PKA). Multidimensional methods of nuclear magnetic resonance (NMR) spectroscopy with high resolution were used to obtain atomicresolution description of structural features and dynamics of unphosphorylated and PKA-phosphorylated MAP2c. Kinetics of phosphorylation by PKA was monitored using fast 2D NMR experiments. Propensities of individual regions of MAP2c to form transient secondary structures were revealed by analyzing chemical shifts of unphosphorylated and PKA-phosphorylated MAP2c. Long-range intramolecular interactions were described by paramagnetic relaxation enhancement, utilizing spin labels attached at different positions in the MAP2c molecule. NMR relaxation experiments provided a detailed picture of internal motions of the MAP2c backbone. Titration with a regulatory 14-3- 3zeta protein revealed its binding sites in unphosphorylated and PKA-phosphorylated MAP2c. The results showed that properties of MAP2c significantly differ from those of the microtubule-associated protein tau, in spite of a high sequence homology of microtubule-binding regions of both proteins.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

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

    2017

  • Confidentiality

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