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We superimposed the modeled RIP1 DD with Fas DD in the Fas DD/FADD DD complex structure.
Therefore, we modeled the RIP1 DD structure based on the structure of Fas DD (PDB id 3OQ9) and mapped the mutations that might disrupt the formation of the RIP1 DD/FADD DD complex on the modeled structure of RIP1 DD.
This finding is consistent with the previous observation that disruption of the type IIb interface on Fas DD did not block formation of the Fas DD/FADD DD complex.
It should be noted that the type IIb surface of RIP1 DD and the type IIa surface of FADD DD do not participate in the assembly of the core 5 5 RIP1 DD/FADD DD complex.
In our model of the RIP1 DD/FADD DD complex, the top layer is formed by five RIP DDs and the bottom layer by five FADD DDs.
The Fas DD/FADD DD complex consists of five to seven Fas DD and five FADD DD molecules in solution.
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The prototype of the DD complexes is the PIDDosome, which consists of RAIDD DD and PIDD DD.
Electron microscopy (EM) of negatively stained RIP1 DD/FADD DD complexes revealed a monodispersed and homogeneous particle population (Supplementary Figure 1).
However, because smaller complexes were never seen in previously studied DD complexes, further investigations are required to address the effects of the D660K mutation at the type IIb interface.
The model of the complete CD95 DISC core structure was assembled on the crystal structure of Apo2L/TRAIL in a complex with death receptor 5 (PDB ID 1dog [52]): CD95 ECD and TM domains were modeled as described above and the model of the CD95 DD domain was based on the CD95 DD crystal structure from the CD95/FADD DDs complex (PDB ID 3ezq [16]).
However, for both the G-DID-DD and DID-DD complexes, we observed molar masses most consistent with formation of tetrameric complexes, i.e. (DID-DD 4/(FH2-DAD)4. DID-DD 4/
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