Difference between revisions of "Part:BBa K4165204"

Revision as of 15:03, 6 October 2022

PHF (Paired Helical Filament)

Insoluble fibers Paired Helical filaments that accumulate id Alzheimer's disease and the other tauopathies.

Usage and Biology

Tau,a microtubule-binding protein, aggregates on itself, decreasing its functionality and being closely linked totauopathies, disorders that are tau-related. Tau aggregation is also closely linked to PHF6 (VQIVYK) and PHF*, two nucleating six-residue segments (VQIINK). Our part, VQIVYK, representing residues 306 to 311 of the tau, is crucial for the full-length protein to form fibrils, and it can also do it on its own. A short sequence motif called PHF6, which may be found near the start of the third internal repeat is necessary for the assembly of tau protein into paired helical filaments (PHFs). This motif's location determines how the protein will form. The most substantial predicted-structure potential in tau is congruent with this motif. Depending on the change in propensity, point mutations in the hexapeptide region can either reduce or increase aggregation. We chose this part as a therapeutic target for AD disease by blocking an additional layer of it.

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]

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 Insoluble fibers Paired Helical filaments that accumulate id Alzheimer's disease and the other tauopathies.
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+Tau,a microtubule-binding protein, aggregates on itself, decreasing its functionality and being closely linked totauopathies, disorders that are tau-related. Tau aggregation is also closely linked to PHF6 (VQIVYK) and PHF*, two nucleating six-residue segments (VQIINK). Our part, VQIVYK, representing residues 306 to 311 of the tau, is crucial for the full-length protein to form fibrils, and it can also do it on its own. A short sequence motif called PHF6, which may be found near the start of the third internal repeat is necessary for the assembly of tau protein into paired helical filaments (PHFs). This motif's location determines how the protein will form. The most substantial predicted-structure potential in tau is congruent with this motif. Depending on the change in propensity, point mutations in the hexapeptide region can either reduce or increase aggregation. We chose this part as a therapeutic target for AD disease by blocking an additional layer of it.
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