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We describe targeting signals in the N-terminal of DAAM1 (distinct from the Dvl2 binding domain) that allows for targeted protein function.
The exotoxins are binary, with the protective antigen acting as the binding domain that allows entry of the toxin into the host cell.
All ETS factors have a winged helix-turn-helix DNA binding domain that allows monomeric binding to the sequence GGA(A/T) [ 3].
Unlike the flavohemoglobins, which contain a flavin adenine dinucleotide (FAD) binding domain that allows for efficient heme redox cycling, proteins such as THB1 would require intermolecular electron transfer to accomplish this last step.
To further investigate the role of oncogenic RAS signaling in the differential induction of cell death in response to DNA damage or proteasome inhibition, we used a 4-hydroxytamoxifen (4OHT -inducible oncogenic RAS fusion protein with estrogen receptor hormone binding domain that allows rapid and titratable induction of downstream signals emanating directly from the mutant RAS protein.
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HMG proteins contain DNA-binding domains that allow them to produce specific changes in target DNA structure [ 2, 3].
TetR and its homologues are not the only transcriptional regulators commonly used to construct genetic circuits, and several classes of transcription factors have modular DNA-binding domains that allow them to be programmed to target a specific nucleotide sequence.
NFκB proteins share a highly conserved, N-terminal, Rel homology domain that allows for DNA binding, dimerization with other NFκB family members, and association with inhibitory, IκB proteins.
Ligand binding to ErbB1 stabilizes a conformation of the extracellular domain that allows receptor dimerization [8].
The interaction between the TF and the DNA involves a certain part of the TF called the TF DNA binding domain that allows the TF to recognize and bind with specific regulatory DNA sequences.
Id proteins have a helix-loop-helix domain that allows them to dimerize with bHLH transcription factors, but lack a DNA-binding domain.
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