Difference between revisions of "Part:BBa K4165205"

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<partinfo>BBa_K4165205 parameters</partinfo>
 
<partinfo>BBa_K4165205 parameters</partinfo>
 
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===References===
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1- Ganguly, P., Do, T. D., Larini, L., LaPointe, N. E., Sercel, A. J., Shade, M. F., Feinstein, S. C., Bowers, M. T., & Shea, J. E. (2015). Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3. The journal of physical chemistry. B, 119(13), 4582–4593. https://doi.org/10.1021/acs.jpcb.5b00175
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2- Seidler, P. M., Boyer, D. R., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Murray, K., ... & Eisenberg, D. S. (2018). Structure-based inhibitors of tau aggregation. Nature chemistry, 10(2), 170-176.

Revision as of 08:19, 7 October 2022


PHF asteric


Structure of the amyloid-spine from microtubule associated protein tau Repeat 2


Usage and Biology

More than 20 neurological diseases, including Alzheimer's disease, are linked to aggregated tau protein. The major parts derive these aggregations are 2 segments of VQIVYK (BBa_K4165205) and our part VQIINK. Previous Researches proved that VQIINK , located at the start of R2 repeat, is the most powerful one for deriving aggregations so many inhibitors can be designed according to this structure for inhibition of these aggregations.

3D Model

                                           Figure 1.: RCSB Figure of PHF6*


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References

1- Ganguly, P., Do, T. D., Larini, L., LaPointe, N. E., Sercel, A. J., Shade, M. F., Feinstein, S. C., Bowers, M. T., & Shea, J. E. (2015). Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3. The journal of physical chemistry. B, 119(13), 4582–4593. https://doi.org/10.1021/acs.jpcb.5b00175

2- Seidler, P. M., Boyer, D. R., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Murray, K., ... & Eisenberg, D. S. (2018). Structure-based inhibitors of tau aggregation. Nature chemistry, 10(2), 170-176.