NMR characterization of intrinsically disordered microtubule associated protein 2c
| Autoři | |
|---|---|
| Rok publikování | 2017 |
| Druh | Konferenční abstrakty |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | 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. |
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