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p(HBP:"proline-rich region 2", pmod(Ph))

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Entity

Name
proline-rich region 2
Namespace
HBP
Namespace Version
20181119
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/90e1cb9e5e882703380c9db8d4915ac6f3cba137/export/hbp-names.belns

Appears in Networks 1

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 5

bp(MESH:"Protein Conformation, alpha-Helical") positiveCorrelation p(HBP:"proline-rich region 2", pmod(Ph)) View Subject | View Object

In this study, we address the structural impact of phosphorylation of the Tau protein by Nuclear Magnetic Resonance (NMR) spectroscopy on a functional fragment of Tau (Tau[Ser208-Ser324] = TauF4). TauF4 was phosphorylated by the proline-directed CDK2/CycA3 kinase on Thr231 (generating the AT180 epitope), Ser235, and equally on Thr212 and Thr217 in the Proline-rich region (Tau[Ser208-Gln244] or PRR). These modifications strongly decrease the capacity of TauF4 to polymerize tubulin into microtubules. While all the NMR parameters are consistent with a globally disordered Tau protein fragment, local clusters of structuration can be defined. The most salient result of our NMR analysis is that phosphorylation in the PRR stabilizes a short α-helix that runs from pSer235 till the very beginning of the microtubule-binding region (Tau[Thr245-Ser324] or MTBR of TauF4). PubMed:22072628

Appears in Networks:

p(HGNC:MAPT, pmod(Ph, Thr, 212)) partOf p(HBP:"proline-rich region 2", pmod(Ph)) View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(Ph, Thr, 217)) partOf p(HBP:"proline-rich region 2", pmod(Ph)) View Subject | View Object

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p(HBP:"proline-rich region 2") hasVariant p(HBP:"proline-rich region 2", pmod(Ph)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ph, Ser, 235)) partOf p(HBP:"proline-rich region 2", pmod(Ph)) View Subject | View Object

Appears in Networks:

Out-Edges 1

p(HBP:"proline-rich region 2", pmod(Ph)) positiveCorrelation bp(MESH:"Protein Conformation, alpha-Helical") View Subject | View Object

In this study, we address the structural impact of phosphorylation of the Tau protein by Nuclear Magnetic Resonance (NMR) spectroscopy on a functional fragment of Tau (Tau[Ser208-Ser324] = TauF4). TauF4 was phosphorylated by the proline-directed CDK2/CycA3 kinase on Thr231 (generating the AT180 epitope), Ser235, and equally on Thr212 and Thr217 in the Proline-rich region (Tau[Ser208-Gln244] or PRR). These modifications strongly decrease the capacity of TauF4 to polymerize tubulin into microtubules. While all the NMR parameters are consistent with a globally disordered Tau protein fragment, local clusters of structuration can be defined. The most salient result of our NMR analysis is that phosphorylation in the PRR stabilizes a short α-helix that runs from pSer235 till the very beginning of the microtubule-binding region (Tau[Thr245-Ser324] or MTBR of TauF4). PubMed:22072628

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.