Difference between revisions of "Part:BBa K4165042"
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===Usage and Biology===
 
===Usage and Biology===
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Switch 21 plays a role in mediating HTRA1's function. For HTRA1 to become active, a conformational modification in the linker is necessary, which displaces the associated inhibitor from the active site. The conformational rearrangement can be mediated through the affinity clamp for tau and beta-amyloid binding. These clamps are used for stabilizing the inhibitor away from the active site. These two domains (inhibitor and affinity clamp connected with linker1 beside with amyloid beta binding peptide connected to tau binding peptide by linker 2). Additionally, (H1A) binding peptide bound to the PDZ domain and connected to the affinity clamp on the other side with linker3.
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Switch 22 plays a role in mediating HTRA1's function. For HTRA1 to become active, a conformational modification in the linker is necessary, which displaces the associated inhibitor from the active site. The conformational rearrangement can be mediated through the affinity clamp for tau and beta-amyloid binding. These clamps are used for stabilizing the inhibitor away from the active site. These two domains (inhibitor and affinity clamp connected with linker1 beside with amyloid beta binding peptide connected to tau binding peptide by linker 2). Additionally, (H1A) binding peptide bound to the PDZ domain and connected to the affinity clamp on the other side with linker3.
  
 
===dry lab===
 
===dry lab===
 
<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
 
<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
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we modeled this switch to see the final structure of the switch, the top model which has score   out of 6 from       .
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we modeled this switch to see the final structure of the switch, the top model which has score 3 out of 6 from TRrosetta.
 
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<p><img src="https:" style="margin-left:200px;" alt="" width="500" /></p>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switch22.png" style="margin-left:200px;" alt="" width="500" /></p>
 
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                                     Figure 1.: The 3D structure of switch21 modeled by
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                                     Figure 1.: The 3D structure of switch22 modeled by TRrosetta.
  
 
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Revision as of 21:46, 7 October 2022


HtrA1 Switch 22

This composite part consists of T7 promoter (BBa_K3633015), lac operator (BBa_K4165062), pGS-21a RBS (BBa_K4165016), 6x His-tag (BBa_K4165020), H1A (BBa_K4165000), GGGGSG Linker (BBa_K4165017), TD28REV, (BBa_K4165006), GGSGGGG Linker (BBa_K4165018), WWW (BBa_K4165007), GGGGSG Linker (BBa_K4165017), WAP inhibitor (BBa_K4165008), and T7 terminator (BBa_K731721).

Usage and Biology

Switch 22 plays a role in mediating HTRA1's function. For HTRA1 to become active, a conformational modification in the linker is necessary, which displaces the associated inhibitor from the active site. The conformational rearrangement can be mediated through the affinity clamp for tau and beta-amyloid binding. These clamps are used for stabilizing the inhibitor away from the active site. These two domains (inhibitor and affinity clamp connected with linker1 beside with amyloid beta binding peptide connected to tau binding peptide by linker 2). Additionally, (H1A) binding peptide bound to the PDZ domain and connected to the affinity clamp on the other side with linker3.

dry lab

Modeling

we modeled this switch to see the final structure of the switch, the top model which has score 3 out of 6 from TRrosetta. 

                                    Figure 1.: The 3D structure of switch22 modeled by TRrosetta.

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
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 538
    Illegal AgeI site found at 274
  • 1000
    COMPATIBLE WITH RFC[1000]