Difference between revisions of "Part:BBa K4165205"
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<partinfo>BBa_K4165205 short</partinfo> | <partinfo>BBa_K4165205 short</partinfo> | ||
| + | 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. | ||
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| + | ===<span class='h3bb'>Sequence and Features</span>=== | ||
| + | <partinfo>BBa_K4165205 SequenceAndFeatures</partinfo> | ||
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/hhh.png" style="margin-left:200px;" alt="" width="500" /></p> | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/hhh.png" style="margin-left:200px;" alt="" width="500" /></p> | ||
</html> | </html> | ||
| − | + | Figure 1.: RCSB Figure of PHF6* Visualized by Pymol. | |
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<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
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<partinfo>BBa_K4165205 parameters</partinfo> | <partinfo>BBa_K4165205 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
| + | ===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 | ||
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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. | ||
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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.