Difference between revisions of "Part:BBa K4165205"
 
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Structure of the amyloid-spine from microtubule-associated protein tau.
  
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Structure of the amyloid-spine from microtubule associated protein tau Repeat 2
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===Usage and Biology===
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More than 20 neurological diseases, including Alzheimer's disease, are linked to aggregated tau protein. The major causes for these aggregations are two segments of VQIVYK (BBa_K4165205) called PHF and our part VQIINK called the PHF*. Previous research proved that VQIINK, located at the start of R2 repeat, is the most powerful one for deriving tau aggregations, so many inhibitors can be designed according to this structure for inhibition of these aggregations, which made it suitable for targeting of the fibrils.
  
  
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===Usage and Biology===
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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.
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===<span class='h3bb'>Sequence and Features</span>===
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<partinfo>BBa_K4165205 SequenceAndFeatures</partinfo>
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===3D Model===
 
===3D Model===
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                                            Figure 1.: RCSB Figure of PHF6*
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                                  Figure 1.: RCSB Figure of PHF6* Visualized by Pymol.
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<span class='h3bb'>Sequence and Features</span>
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Latest revision as of 09:03, 13 October 2022


PHF asteric

Structure of the amyloid-spine from microtubule-associated protein tau.

Usage and Biology

More than 20 neurological diseases, including Alzheimer's disease, are linked to aggregated tau protein. The major causes for these aggregations are two segments of VQIVYK (BBa_K4165205) called PHF and our part VQIINK called the PHF*. Previous research proved that VQIINK, located at the start of R2 repeat, is the most powerful one for deriving tau aggregations, so many inhibitors can be designed according to this structure for inhibition of these aggregations, which made it suitable for targeting of the fibrils.


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]


3D Model

                                  Figure 1.: RCSB Figure of PHF6* Visualized by Pymol.

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.